Glycosylated Iminosugars: Isolation, Synthesis and Biological Activities

doi:10.7536/PC190307

In this paper, the separation, synthesis and biological activities of glycosylated iminosugars are systematically summarized. The naturally occurring glycosylated iminosugar products can be classified into five types according to their iminosugar units. Most of them have important biological activities, especially glycosidase inhibitory activities. Potential pharmacological activities of these compounds promote the study of synthetic strategies. According to the construction methods of glycoside bonds, these strategies can be roughly divided into enzyme catalyzed transglycosylation and chemical synthesis, of which the main difference is reaction condition. Enzyme catalyzed transglycosylation features mild reaction conditions and possible avoidance of protection groups, but the reaction efficiency and selectivity still need further improvement. Many synthetic strategies for ordinary glycosides can be used in chemical synthesis of glycosylated iminosugars, and are applicable for almost all synthetic targets. However, burdensome protection-deprotection procedures pull down the efficiency of chemical synthesis. The development of synthetic strategies have promoted the design and synthesis of the natural products and their analogues, which greatly enriches the variety and biological activities of glycosylated iminosugars. Generally, biological activities of glycosylated iminosugars are influenced by both the glycosyl groups and the iminosugar units. As the cross-domain of traditional carbohydrate chemistry and iminosugar chemistry, the structural diversity of glycosylated iminosugars provides excellent parent skeletons for the development of highly active and selective lead compounds, which endows these compounds with potential applications in drug discovery.

Key words: iminosugar, azasugar, glycosylated, synthesis, biological activity, structure-activity relationship

Fig. 1 Some representative iminosugars

Fig. 2 Approved iminosugar drugs

Table 1 Naturally occurring glycosides of iminosugars and their biological activities

Biological activities		Source and Reference
Rat intestinal sucrase-IC₅₀0.8 μM^[10] Rat intestinal maltase-IC₅₀4.4 μM^[11] Rice α-glucosidase-IC₅₀ 0.95 μM^[11]		Root bark, dry fruits and leaves of mulberry trees(Morus alba L.)^{[10, 11]} and Leaves of Morus bombycis^[21]
Rice α-glucosidase-IC₅₀ 1.6 μM^[22] Trehalase(porcine kidney)-5.6 μM^[22]		Root bark of mulberry trees(Morus alba L.)^{[10, 11]}
Rat intestinal sucrase-IC₅₀0.79 μM^[22]		Root bark of mulberry trees(Morus alba L.)^[11]
Rat intestinal sucrase-IC₅₀0.31 μM^[11] Rat intestinal maltase-IC₅₀1.7 μM^[11] Rat intestinal palatinase-IC₅₀0.23 μM^[11] Rice α-glucosidase-IC₅₀30 μM^[11]		Root bark of mulberry trees(Morus alba L.)^{[10, 11]}
Rat intestinal sucrase-IC₅₀0.35 μM^[22] Rat intestinal palatinase-IC₅₀0.90 μM^[22] Rice α-glucosidase-IC₅₀34 nM^[22]		Root bark of mulberry trees(Morus alba L.)^[11] and bulbs of Scilla sibirica^[23]
Rat intestinal sucrase-IC₅₀2.5 μM^[22] Rat intestinal palatinase-IC₅₀2.7 μM^[22] Rice α-glucosidase-IC₅₀22 μM^[22]		Root bark of mulberry trees(Morus alba L.)^{[10, 11]}
Rat intestinal maltase-IC₅₀2.3 μM^[22] Rat intestinal sucrase-IC₅₀0.40 μM^[22] Rat intestinal palatinase-IC₅₀0.47 μM^[22] Rice α-glucosidase-IC₅₀0.61 μM^[22]		Root bark of mulberry trees(Morus alba L.)^[11] and P. acidophila^[24]
Rat intestinal sucrase-IC₅₀940 μM^[10] Rat intestinal palatinase- IC₅₀31 μM^[11]		Root bark, dry fruits and leaves of mulberry trees(Morus alba L.)^{[10, 11]}
Rat intestinal sucrase-IC₅₀35 μM^[11] Rat intestinal maltase-IC₅₀40 μM^[11] Rice α-glucosidase-IC₅₀6.0 μM^[11]		Root bark of mulberry trees(Morus alba L.)^[11]
No inhibition towards α-L-fucosidase^[25]		Roots of Stemona tuberosa^[25]
No inhibition towards α-L-fucosidase^[25]		Roots of Stemona tuberosa^[25]
No inhibition towards α-L-fucosidase^[25]		Roots of Stemona tuberosa^[25]
No inhibition towards α-L-fucosidase^[25]		Roots of Stemona tuberosa^[25]
Crude rat intestinal α-glucosidase-IC₅₀4.22 μM^[26] Rice α-glucosidase-IC₅₀0.25 μM^[12] Trehalase(porcine kidney)-IC₅₀13 nM^[12]		Whole plant of Lobelia sessilifolia(Campanulaceae)^[12], roots of Stemona tuberosa^[25], leaves of Suregada glomerulata^[26], whole plant of Aglaonema treubii^[27] and bulbs of Hyacinthus orientalis^[28]
Crude rat intestinal α-glucosidase-IC₅₀38.55 μM^[26]		Leaves of Suregada glomerulata^[26]
Crude rat intestinal α-glucosidase-IC₅₀24.34 μM^[26]		Leaves of Suregada glomerulata^[26]
ND^a		Leaves of Suregada glomerulata^[26] and whole plant of Aglaonema treubii^[27]
ND		Leaves of Suregada glomerulata^[26]
Trehalase(porcine kidney)-53 μM^[12]	Roots of Adenophora spp. (Campanulaceae)^[12]
Rice α-glucosidase-IC₅₀0.49 μM^[12] Rat intestinal sucrase-IC₅₀2.4 μM^[12] Rat intestinal maltase-IC₅₀6.1 μM^[12] Rat intestinal isomaltase-IC₅₀2.1 μM^[12] α-Galactosidase(coffee bean)-IC₅₀1.7 μM^[12]		Roots of Adenophora spp. (Campanulaceae)^[12]
NI^b[29] Intraperitoneal administration of 150 μmol/kg of 30 had no effect on the blood glucose levels in STZ-diabetic mice^[30]		Leave sand roots of Xanthocercis zambesiaca(Leguminosae)^{[29, 30]}
NI^[29] 31 can reduce the blood glucose level after ip injection of 150 μmol/kg^[30]		Leave sand roots of Xanthocercis zambesiaca(Leguminosae)^{[29, 30]} and seeds of Xanthocercis zambesiaca (Leguminosae)^[31]
ND		Cyclamen coum^[32]
NI^[33]		Aerial parts of Lycopodiastrum casuarinoides^[33]
36a: Silk worm maltase-IC₅₀530 μM^[10] NI^[34] 36b: NI^[34]		36a: Root bark, dry fruits and leaves of mulberry trees and silkworms(Morus alba L.)^{[10, 11]}, leaves of Morus bombycis^[21] and pods of Angylocalyx pynaertii^[34] 36b: Pods of Angylocalyx pynaertii^[34]
α-Glucosidase(rice)-IC₅₀0.79 μM^[35] Rat intestinal maltase-IC₅₀4.7 μM^[35] Rat intestinal isomaltase-IC₅₀12 μM^[35] Rat intestinal sucrase-IC₅₀5.0 μM^[35] β-Glucosidase(bovine liver)-IC₅₀850 μM^[35] β-Galactosidase(bovine liver)-IC₅₀270 μM;^[25] IC₅₀465 μM^[35] Trehalase(porcine kidney)-IC₅₀NI^[35]		Roots of Stemona tuberosa^[25] and dry leaves of Baphia nitida^[35]
α-Glucosidase(rice)-IC₅₀22 μM^[35] Rat intestinal maltase-IC₅₀65 μM^[35] Rat intestinal isomaltase-IC₅₀136 μM^[35] Rat intestinal sucrase-IC₅₀57 μM^[35] β-Glucosidase(bovine liver)-IC₅₀ NI^[35] β-Galactosidase(bovine liver)-IC₅₀NI^[35] Trehalase(porcine kidney)-IC₅₀26 μM^[35]		Dry leaves of Baphia nitida^[35]
β-Galactosidase(bovine liver)-IC₅₀40 μM^[14] Rat intestinal lactase-IC₅₀1.6 μM^[14]		Immature fruits and stalks of bluebell(Hyacinthoides non-scripta) and bulbs of Scilla campanulata(Hyacinthaceae)^[14] and leaves of bluebell(Hyacinthoides non-scripta)^[36]
β-Glucosidase(almond)-IC₅₀4.6 μM^[14] β-Glucosidase(C. saccharolyticum)-IC₅₀0.34 μM^[14] β-Galactosidase(bovine liver)-IC₅₀24 μM^[14] Rat intestinal lactase-IC₅₀0.18 μM^[14]		Immature fruits and stalks of bluebell(Hyacinthoides non-scripta) and bulbs of Scilla campanulata(Hyacinthaceae)^[14]
	β-Mannosidase(rat epididymis)-IC₅₀160 μM^[23] α-L-fucosidase(bovine epididymis)-IC₅₀78 μM^[23]		Bulbs of Scilla sibirica^[23]
	β-Mannosidase(rat epididymis)-IC₅₀180 μM^[23] α-L-fucosidase(bovine epididymis)-IC₅₀13 μM^[23]		Bulbs of Scilla sibirica^[23]
	NI^[37]		Dry branches of Broussonetia kazinoki SIEB.(Moraceae)^[37]
	NI^[37]		Dry branches of Broussonetia kazinoki SIEB.(Moraceae)^[37]
	β-Glucosidase(sweet almond)-IC₅₀26 nM^[15] β-Galactosidase(bovine liver)-IC₅₀5 nM^[15] β-Mannosidase(snail acetone powder)- IC₅₀0.30 μM^[15]		Dry branches of Broussonetia kazinoki SIEB.(Moraceae)^[15]
	β-Glucosidase(sweet almond)-IC₅₀17 nM^[15] β-Galactosidase(bovine liver)-IC₅₀4 nM^[15] β-Mannosidase(snail acetone powder)- IC₅₀0.20 μM^[15]		Dry branches of Broussonetia kazinoki SIEB.(Moraceae)^[15]
	β-Glucosidase(sweet almond)-IC₅₀1.4 μM^[38] β-Galactosidase(bovine liver)-IC₅₀0.60 μM^[38] β-Mannosidase(snail acetone powder)- IC₅₀20.0 μM^[38]		Dry branches of Broussonetia kazinoki SIEB.(Moraceae)^[38]
	ND		Dry branches of Broussonetia kazinoki SIEB.(Moraceae)^[39]
	β-Glucosidase(bovine liver)-IC₅₀222 μM^[40] α-Galactosidase(coffee bean)-IC₅₀8 μM^[40]		Roots of A. triphylla var. japonica^[40]
	β-Glucuronidase-IC₅₀560 μM^[41]		Cultured filamentous cyanobacterium Anabaena sp.^[41]
	51: Competitive inhibitor of metallo-β-lactamase BceII from Bacillus cereus in its two-zinc form.^[42] Compounds 51~53 are potent β-lactam synergists^{[8, 43, 44]}		51: Pseudomonas acidophila^[8] and Pseudomonas mesoacidophila^[43] 52, 53: Pseudomonas mesoacidophila^[43]
	Potentiators of β-lactam antibiotics^{[45, 46]}		Culture broth of Chromobacterium violaceum^{[45, 47]}
	Potentiators of β-lactam antibiotics^{[45, 46]}		Culture broth of Chromobacterium violaceum^{[45, 47]}
	α-Glucosidase(rice)-IC₅₀1.2 μM^[18] Rat intestinal maltase-IC₅₀0.7 μM^[18] Rat intestinal isomaltase-IC₅₀3.9 μM^[18] Trehalase(porcine kidney)-IC₅₀12 μM^[18] Glucoamylase(aspergillus niger)-IC₅₀4.4 μM^[17]; 0.7 μM^[18]		Bark of Casuarina equisetifolia L. and leaves of Eugenia jambolana Lam.^[48] and Fresh bark of Syzygium malaccense L.^[49]
	α-Glucosidase(rice)-IC₅₀1.8 μM^[18] α-Glucosidase(yeast)-IC₅₀1.6 μM^[18] Rat intestinal maltase-IC₅₀41 μM^[18] Rat intestinal isomaltase-IC₅₀2.9 μM^[18]		Seeds of C. australe^[18]
	Rat intestinal sucrase-IC₅₀ 0.4 μM^[19] Lysosomal α-glucosidase-IC₅₀ > 400 μM^[19]		Seeds of C. australe^[18]
	α-Glucosidase(caldocellum saccharolyticum)- IC₅₀190 μM^[10] α-Galactosidase(coffee beans)-IC₅₀150 μM^[10] Trehalase(porcine kidney)-1000 μM^[10]		Dry fruits and leaves of mulberry trees(Morus alba L.)^{[10, 50]}
	Rice α-glucosidase-IC₅₀1.9 μM^[20]		Fruits of Nicandra physalodes Boehm.(Solanaceae)^[51]

Table 1 Naturally occurring glycosides of iminosugars and their biological activities

Biological activities		Source and Reference
Rat intestinal sucrase-IC₅₀0.8 μM^[10] Rat intestinal maltase-IC₅₀4.4 μM^[11] Rice α-glucosidase-IC₅₀ 0.95 μM^[11]		Root bark, dry fruits and leaves of mulberry trees(Morus alba L.)^{[10, 11]} and Leaves of Morus bombycis^[21]
Rice α-glucosidase-IC₅₀ 1.6 μM^[22] Trehalase(porcine kidney)-5.6 μM^[22]		Root bark of mulberry trees(Morus alba L.)^{[10, 11]}
Rat intestinal sucrase-IC₅₀0.79 μM^[22]		Root bark of mulberry trees(Morus alba L.)^[11]
Rat intestinal sucrase-IC₅₀0.31 μM^[11] Rat intestinal maltase-IC₅₀1.7 μM^[11] Rat intestinal palatinase-IC₅₀0.23 μM^[11] Rice α-glucosidase-IC₅₀30 μM^[11]		Root bark of mulberry trees(Morus alba L.)^{[10, 11]}
Rat intestinal sucrase-IC₅₀0.35 μM^[22] Rat intestinal palatinase-IC₅₀0.90 μM^[22] Rice α-glucosidase-IC₅₀34 nM^[22]		Root bark of mulberry trees(Morus alba L.)^[11] and bulbs of Scilla sibirica^[23]
Rat intestinal sucrase-IC₅₀2.5 μM^[22] Rat intestinal palatinase-IC₅₀2.7 μM^[22] Rice α-glucosidase-IC₅₀22 μM^[22]		Root bark of mulberry trees(Morus alba L.)^{[10, 11]}
Rat intestinal maltase-IC₅₀2.3 μM^[22] Rat intestinal sucrase-IC₅₀0.40 μM^[22] Rat intestinal palatinase-IC₅₀0.47 μM^[22] Rice α-glucosidase-IC₅₀0.61 μM^[22]		Root bark of mulberry trees(Morus alba L.)^[11] and P. acidophila^[24]
Rat intestinal sucrase-IC₅₀940 μM^[10] Rat intestinal palatinase- IC₅₀31 μM^[11]		Root bark, dry fruits and leaves of mulberry trees(Morus alba L.)^{[10, 11]}
Rat intestinal sucrase-IC₅₀35 μM^[11] Rat intestinal maltase-IC₅₀40 μM^[11] Rice α-glucosidase-IC₅₀6.0 μM^[11]		Root bark of mulberry trees(Morus alba L.)^[11]
No inhibition towards α-L-fucosidase^[25]		Roots of Stemona tuberosa^[25]
No inhibition towards α-L-fucosidase^[25]		Roots of Stemona tuberosa^[25]
No inhibition towards α-L-fucosidase^[25]		Roots of Stemona tuberosa^[25]
No inhibition towards α-L-fucosidase^[25]		Roots of Stemona tuberosa^[25]
Crude rat intestinal α-glucosidase-IC₅₀4.22 μM^[26] Rice α-glucosidase-IC₅₀0.25 μM^[12] Trehalase(porcine kidney)-IC₅₀13 nM^[12]		Whole plant of Lobelia sessilifolia(Campanulaceae)^[12], roots of Stemona tuberosa^[25], leaves of Suregada glomerulata^[26], whole plant of Aglaonema treubii^[27] and bulbs of Hyacinthus orientalis^[28]
Crude rat intestinal α-glucosidase-IC₅₀38.55 μM^[26]		Leaves of Suregada glomerulata^[26]
Crude rat intestinal α-glucosidase-IC₅₀24.34 μM^[26]		Leaves of Suregada glomerulata^[26]
ND^a		Leaves of Suregada glomerulata^[26] and whole plant of Aglaonema treubii^[27]
ND		Leaves of Suregada glomerulata^[26]
Trehalase(porcine kidney)-53 μM^[12]	Roots of Adenophora spp. (Campanulaceae)^[12]
Rice α-glucosidase-IC₅₀0.49 μM^[12] Rat intestinal sucrase-IC₅₀2.4 μM^[12] Rat intestinal maltase-IC₅₀6.1 μM^[12] Rat intestinal isomaltase-IC₅₀2.1 μM^[12] α-Galactosidase(coffee bean)-IC₅₀1.7 μM^[12]		Roots of Adenophora spp. (Campanulaceae)^[12]
NI^b[29] Intraperitoneal administration of 150 μmol/kg of 30 had no effect on the blood glucose levels in STZ-diabetic mice^[30]		Leave sand roots of Xanthocercis zambesiaca(Leguminosae)^{[29, 30]}
NI^[29] 31 can reduce the blood glucose level after ip injection of 150 μmol/kg^[30]		Leave sand roots of Xanthocercis zambesiaca(Leguminosae)^{[29, 30]} and seeds of Xanthocercis zambesiaca (Leguminosae)^[31]
ND		Cyclamen coum^[32]
NI^[33]		Aerial parts of Lycopodiastrum casuarinoides^[33]
36a: Silk worm maltase-IC₅₀530 μM^[10] NI^[34] 36b: NI^[34]		36a: Root bark, dry fruits and leaves of mulberry trees and silkworms(Morus alba L.)^{[10, 11]}, leaves of Morus bombycis^[21] and pods of Angylocalyx pynaertii^[34] 36b: Pods of Angylocalyx pynaertii^[34]
α-Glucosidase(rice)-IC₅₀0.79 μM^[35] Rat intestinal maltase-IC₅₀4.7 μM^[35] Rat intestinal isomaltase-IC₅₀12 μM^[35] Rat intestinal sucrase-IC₅₀5.0 μM^[35] β-Glucosidase(bovine liver)-IC₅₀850 μM^[35] β-Galactosidase(bovine liver)-IC₅₀270 μM;^[25] IC₅₀465 μM^[35] Trehalase(porcine kidney)-IC₅₀NI^[35]		Roots of Stemona tuberosa^[25] and dry leaves of Baphia nitida^[35]
α-Glucosidase(rice)-IC₅₀22 μM^[35] Rat intestinal maltase-IC₅₀65 μM^[35] Rat intestinal isomaltase-IC₅₀136 μM^[35] Rat intestinal sucrase-IC₅₀57 μM^[35] β-Glucosidase(bovine liver)-IC₅₀ NI^[35] β-Galactosidase(bovine liver)-IC₅₀NI^[35] Trehalase(porcine kidney)-IC₅₀26 μM^[35]		Dry leaves of Baphia nitida^[35]
β-Galactosidase(bovine liver)-IC₅₀40 μM^[14] Rat intestinal lactase-IC₅₀1.6 μM^[14]		Immature fruits and stalks of bluebell(Hyacinthoides non-scripta) and bulbs of Scilla campanulata(Hyacinthaceae)^[14] and leaves of bluebell(Hyacinthoides non-scripta)^[36]
β-Glucosidase(almond)-IC₅₀4.6 μM^[14] β-Glucosidase(C. saccharolyticum)-IC₅₀0.34 μM^[14] β-Galactosidase(bovine liver)-IC₅₀24 μM^[14] Rat intestinal lactase-IC₅₀0.18 μM^[14]		Immature fruits and stalks of bluebell(Hyacinthoides non-scripta) and bulbs of Scilla campanulata(Hyacinthaceae)^[14]
	β-Mannosidase(rat epididymis)-IC₅₀160 μM^[23] α-L-fucosidase(bovine epididymis)-IC₅₀78 μM^[23]		Bulbs of Scilla sibirica^[23]
	β-Mannosidase(rat epididymis)-IC₅₀180 μM^[23] α-L-fucosidase(bovine epididymis)-IC₅₀13 μM^[23]		Bulbs of Scilla sibirica^[23]
	NI^[37]		Dry branches of Broussonetia kazinoki SIEB.(Moraceae)^[37]
	NI^[37]		Dry branches of Broussonetia kazinoki SIEB.(Moraceae)^[37]
	β-Glucosidase(sweet almond)-IC₅₀26 nM^[15] β-Galactosidase(bovine liver)-IC₅₀5 nM^[15] β-Mannosidase(snail acetone powder)- IC₅₀0.30 μM^[15]		Dry branches of Broussonetia kazinoki SIEB.(Moraceae)^[15]
	β-Glucosidase(sweet almond)-IC₅₀17 nM^[15] β-Galactosidase(bovine liver)-IC₅₀4 nM^[15] β-Mannosidase(snail acetone powder)- IC₅₀0.20 μM^[15]		Dry branches of Broussonetia kazinoki SIEB.(Moraceae)^[15]
	β-Glucosidase(sweet almond)-IC₅₀1.4 μM^[38] β-Galactosidase(bovine liver)-IC₅₀0.60 μM^[38] β-Mannosidase(snail acetone powder)- IC₅₀20.0 μM^[38]		Dry branches of Broussonetia kazinoki SIEB.(Moraceae)^[38]
	ND		Dry branches of Broussonetia kazinoki SIEB.(Moraceae)^[39]
	β-Glucosidase(bovine liver)-IC₅₀222 μM^[40] α-Galactosidase(coffee bean)-IC₅₀8 μM^[40]		Roots of A. triphylla var. japonica^[40]
	β-Glucuronidase-IC₅₀560 μM^[41]		Cultured filamentous cyanobacterium Anabaena sp.^[41]
	51: Competitive inhibitor of metallo-β-lactamase BceII from Bacillus cereus in its two-zinc form.^[42] Compounds 51~53 are potent β-lactam synergists^{[8, 43, 44]}		51: Pseudomonas acidophila^[8] and Pseudomonas mesoacidophila^[43] 52, 53: Pseudomonas mesoacidophila^[43]
	Potentiators of β-lactam antibiotics^{[45, 46]}		Culture broth of Chromobacterium violaceum^{[45, 47]}
	Potentiators of β-lactam antibiotics^{[45, 46]}		Culture broth of Chromobacterium violaceum^{[45, 47]}
	α-Glucosidase(rice)-IC₅₀1.2 μM^[18] Rat intestinal maltase-IC₅₀0.7 μM^[18] Rat intestinal isomaltase-IC₅₀3.9 μM^[18] Trehalase(porcine kidney)-IC₅₀12 μM^[18] Glucoamylase(aspergillus niger)-IC₅₀4.4 μM^[17]; 0.7 μM^[18]		Bark of Casuarina equisetifolia L. and leaves of Eugenia jambolana Lam.^[48] and Fresh bark of Syzygium malaccense L.^[49]
	α-Glucosidase(rice)-IC₅₀1.8 μM^[18] α-Glucosidase(yeast)-IC₅₀1.6 μM^[18] Rat intestinal maltase-IC₅₀41 μM^[18] Rat intestinal isomaltase-IC₅₀2.9 μM^[18]		Seeds of C. australe^[18]
	Rat intestinal sucrase-IC₅₀ 0.4 μM^[19] Lysosomal α-glucosidase-IC₅₀ > 400 μM^[19]		Seeds of C. australe^[18]
	α-Glucosidase(caldocellum saccharolyticum)- IC₅₀190 μM^[10] α-Galactosidase(coffee beans)-IC₅₀150 μM^[10] Trehalase(porcine kidney)-1000 μM^[10]		Dry fruits and leaves of mulberry trees(Morus alba L.)^{[10, 50]}
	Rice α-glucosidase-IC₅₀1.9 μM^[20]		Fruits of Nicandra physalodes Boehm.(Solanaceae)^[51]

Table 2 Glycosides of iminosugars synthesized by enzymatic method and their biological activities

Compounds		Biological activities			Ref
		Golgi endomannosidase-IC₅₀1.7 μM^[52]			52~54
		Weak golgi endomannosidase inhibitor^[53]			53
		Weak inhibitory activities towards cellulases^[55]			55, 56
		Improved inhibition against cyclodextrin glycosyltransferase and sharply decreased inhibition towards glucoamylase comparing to their corresponding N-substituted moranolines^[57]. n=0, CGT-ase-IC₅₀46 μM^[57] Glucoamylase-IC₅₀>1000 μM^[57] n=1, CGT-ase-IC₅₀38 μM^[57] Glucoamylase-IC₅₀320 μM^[57] n=2 or 3, CGT-ase-IC₅₀250 μM^[57] Glucoamylase-IC₅₀>1000 μM^[57] n=4 or 5, CGT-ase-IC₅₀260 μM^[57] Glucoamylase-IC₅₀>1000 μM^[57] n=6, CGT-ase-IC₅₀180 μM^[57] Glucoamylase-IC₅₀>1000 μM^[57]			57
		CGT-ase-IC₅₀450 μM^[57] Glucoamylase-IC₅₀>1000 μM^[57]			57
		n=1, CGT-ase-IC₅₀500 μM^[57] Glucoamylase-IC₅₀>1000 μM^[57] n=2, CGT-ase-IC₅₀>1000 μM^[57] Glucoamylase-IC₅₀>1000 μM^[57] n=3, CGT-ase-IC₅₀290 μM^[57] Glucoamylase-IC₅₀>1000 μM^[57]			57
		n=2, CGT-ase-IC₅₀50 μM^[57] Glucoamylase-IC₅₀>1000 μM^[57] n=3, CGT-ase-IC₅₀520 μM^[57] Glucoamylase-IC₅₀>1000 μM^[57] n=4, CGT-ase-IC₅₀60 μM^[57] Glucoamylase-IC₅₀>1000 μM^[57]			57
		ND^a			58
		ND			58~61
		ND			58
		ND			58
		Potent inhibitor of the cellulases tested^[55]			55
		Weak inhibitory activities towards cellulases^[55]			55
		73: Endo-glycanase cex(cellulomonas fimi)-K_i2.0 μM^[62] Cel5A( Bacillus agaradhaerens)-K_i0.7 μM^[63] 74: Endo-glycanase cex(cellulomonas fimi)-K_i0.8 μM^[62] Cel5A( Bacillus agaradhaerens)-K_i5 nM^[63] 75: Endo-glycanase cex(cellulomonas fimi)-K_i0.6 μM^[62] Cel5A( Bacillus agaradhaerens)-K_i400 nM^[63] 76: Endo-glycanase cex(cellulomonas fimi)-K_i1900 μM^[62] 77: Endo-glycanase cex(cellulomonas fimi)-K_i1000 μM^[62] Endo-β-1,4-(xylo)glucan hydrolase ( Paenibacillus polymyxa)-IC₅₀7 μM^[64] 78: Endo-glycanase cex(cellulomonas fimi)-K_i80 μM^[62]			62
		79: Xylanase(Bacillus circulans)-K_i1500 μM^{[65, 66]} Xylanase(cellulomonas fimi)-K_i5.8 μM^{[65, 66]} 80: Endo-glycanase cex(cellulomonas fimi)-K_i88±6 μM^[65] Cel5A( Bacillus agaradhaerens)-K_i0.16±0.03 μM^[65] 81: Endo-glycanase cex(cellulomonas fimi)-K_i1100 μM^{[65, 66]} Cel5A( Bacillus agaradhaerens)-K_i0.13 μM^{[65, 66]} 82: Endo-glycanase cex(cellulomonas fimi)-K_i63±4 μM^[65] Cel5A( Bacillus agaradhaerens)-K_i0. 018±0.002 μM^[65]			65
		HPA: human pancreaticα-amylase HSA: human salivary α-amylase n=1, HPA-IC₅₀2.5 mM^[67] n=2, HPA-IC₅₀43 μM^[67] HSA-IC₅₀2.0 mM^[67] HSA-IC₅₀82 μM^[67] Rat maltase-NI^[67] Rat maltase-NI^[67] n=3, HPA-IC₅₀30 μM^[67] n=4, HPA-IC₅₀0.23 mM^[67] HSA-IC₅₀49 μM^[67] HSA-IC₅₀0.36 mM^[67] Rat maltase-NI^[67] Rat maltase-NI^[67]			67
		n=1, HPA-IC₅₀3.0 mM^[67] n=2, HPA-IC₅₀34 μM^[67] HSA-IC₅₀2.0 mM^[67] HSA-IC₅₀46 μM^[67] Rat maltase-IC₅₀1.0 mM^[67] Rat maltase-NI^[67] n=3, HPA-IC₅₀25 μM^[67] n=4, HPA-IC₅₀70 μM^[67] HSA-IC₅₀42 μM^[67] HSA-IC₅₀70 μM^[67] Rat maltase-NI^[67] Rat maltase-NI^[67]			67
		No inhibitory activities towards HPA,HSA and rat maltase^[67]			67
		NI^b[20]			20
		α-Galactosidase(green coffee bean)-IC₅₀26 μM^[20] Weak inhibitor of β-glucosidase, β-galactosidase, trehalase^[20]			20
		α-Galactosidase(green coffee bean)-IC₅₀80 μM^[20] Trehalase(porcine kidney)-IC₅₀34 μM^[20]			20
		ND			68

Table 2 Glycosides of iminosugars synthesized by enzymatic method and their biological activities

Compounds		Biological activities			Ref
		Golgi endomannosidase-IC₅₀1.7 μM^[52]			52~54
		Weak golgi endomannosidase inhibitor^[53]			53
		Weak inhibitory activities towards cellulases^[55]			55, 56
		Improved inhibition against cyclodextrin glycosyltransferase and sharply decreased inhibition towards glucoamylase comparing to their corresponding N-substituted moranolines^[57]. n=0, CGT-ase-IC₅₀46 μM^[57] Glucoamylase-IC₅₀>1000 μM^[57] n=1, CGT-ase-IC₅₀38 μM^[57] Glucoamylase-IC₅₀320 μM^[57] n=2 or 3, CGT-ase-IC₅₀250 μM^[57] Glucoamylase-IC₅₀>1000 μM^[57] n=4 or 5, CGT-ase-IC₅₀260 μM^[57] Glucoamylase-IC₅₀>1000 μM^[57] n=6, CGT-ase-IC₅₀180 μM^[57] Glucoamylase-IC₅₀>1000 μM^[57]			57
		CGT-ase-IC₅₀450 μM^[57] Glucoamylase-IC₅₀>1000 μM^[57]			57
		n=1, CGT-ase-IC₅₀500 μM^[57] Glucoamylase-IC₅₀>1000 μM^[57] n=2, CGT-ase-IC₅₀>1000 μM^[57] Glucoamylase-IC₅₀>1000 μM^[57] n=3, CGT-ase-IC₅₀290 μM^[57] Glucoamylase-IC₅₀>1000 μM^[57]			57
		n=2, CGT-ase-IC₅₀50 μM^[57] Glucoamylase-IC₅₀>1000 μM^[57] n=3, CGT-ase-IC₅₀520 μM^[57] Glucoamylase-IC₅₀>1000 μM^[57] n=4, CGT-ase-IC₅₀60 μM^[57] Glucoamylase-IC₅₀>1000 μM^[57]			57
		ND^a			58
		ND			58~61
		ND			58
		ND			58
		Potent inhibitor of the cellulases tested^[55]			55
		Weak inhibitory activities towards cellulases^[55]			55
		73: Endo-glycanase cex(cellulomonas fimi)-K_i2.0 μM^[62] Cel5A( Bacillus agaradhaerens)-K_i0.7 μM^[63] 74: Endo-glycanase cex(cellulomonas fimi)-K_i0.8 μM^[62] Cel5A( Bacillus agaradhaerens)-K_i5 nM^[63] 75: Endo-glycanase cex(cellulomonas fimi)-K_i0.6 μM^[62] Cel5A( Bacillus agaradhaerens)-K_i400 nM^[63] 76: Endo-glycanase cex(cellulomonas fimi)-K_i1900 μM^[62] 77: Endo-glycanase cex(cellulomonas fimi)-K_i1000 μM^[62] Endo-β-1,4-(xylo)glucan hydrolase ( Paenibacillus polymyxa)-IC₅₀7 μM^[64] 78: Endo-glycanase cex(cellulomonas fimi)-K_i80 μM^[62]			62
		79: Xylanase(Bacillus circulans)-K_i1500 μM^{[65, 66]} Xylanase(cellulomonas fimi)-K_i5.8 μM^{[65, 66]} 80: Endo-glycanase cex(cellulomonas fimi)-K_i88±6 μM^[65] Cel5A( Bacillus agaradhaerens)-K_i0.16±0.03 μM^[65] 81: Endo-glycanase cex(cellulomonas fimi)-K_i1100 μM^{[65, 66]} Cel5A( Bacillus agaradhaerens)-K_i0.13 μM^{[65, 66]} 82: Endo-glycanase cex(cellulomonas fimi)-K_i63±4 μM^[65] Cel5A( Bacillus agaradhaerens)-K_i0. 018±0.002 μM^[65]			65
		HPA: human pancreaticα-amylase HSA: human salivary α-amylase n=1, HPA-IC₅₀2.5 mM^[67] n=2, HPA-IC₅₀43 μM^[67] HSA-IC₅₀2.0 mM^[67] HSA-IC₅₀82 μM^[67] Rat maltase-NI^[67] Rat maltase-NI^[67] n=3, HPA-IC₅₀30 μM^[67] n=4, HPA-IC₅₀0.23 mM^[67] HSA-IC₅₀49 μM^[67] HSA-IC₅₀0.36 mM^[67] Rat maltase-NI^[67] Rat maltase-NI^[67]			67
		n=1, HPA-IC₅₀3.0 mM^[67] n=2, HPA-IC₅₀34 μM^[67] HSA-IC₅₀2.0 mM^[67] HSA-IC₅₀46 μM^[67] Rat maltase-IC₅₀1.0 mM^[67] Rat maltase-NI^[67] n=3, HPA-IC₅₀25 μM^[67] n=4, HPA-IC₅₀70 μM^[67] HSA-IC₅₀42 μM^[67] HSA-IC₅₀70 μM^[67] Rat maltase-NI^[67] Rat maltase-NI^[67]			67
		No inhibitory activities towards HPA,HSA and rat maltase^[67]			67
		NI^b[20]			20
		α-Galactosidase(green coffee bean)-IC₅₀26 μM^[20] Weak inhibitor of β-glucosidase, β-galactosidase, trehalase^[20]			20
		α-Galactosidase(green coffee bean)-IC₅₀80 μM^[20] Trehalase(porcine kidney)-IC₅₀34 μM^[20]			20
		ND			68

Scheme. 1 Synthesis of 4-O-α-D-glucopyranosyl-DNJ by enzymatic method[56]

Scheme. 2 Synthesis of α- or β- glucosylated DNJ derivatives by enzymatic method[22]

Table 3 Concentrations of glucosides of DNJ giving 50% inhibition of glycosidase activities(μM)

Enzymes	IC₅₀(μM)
	DNJ	11	14	16	12	15
	R₁=H, R₂=H, R₃=H^a	R₁=α-Glc, R₂=H, R₃=H	R₁=H, R₂=α-Glc, R₃=H	R₁=H, R₂=H, R₃=α-Glc	R₁=β-Glc, R₂=H, R₃=H	R₁=H, R₂=H, R₃=β-Glc
Rat intestinal maltose	0.36	24	5.2	2.3	4.0	24
Rat intestinal sucrose	0.21	2.4	0.35	0.4	0.79	2.5
Rat intestinal palatinose	0.3	6.2	0.9	0.47	1.4	2.7
Rat intestinal trehalose	42	2.2	NI	NI	NI	NI
Rat intestinal cellobiose	520	NI^b	NI	NI	NI	NI
Rat intestinal lactose	34	NI	NI	NI	520	460
α-Glucosidase Baker’s yeast Rice Rat liver lysosome	330 0.05 0.4	NI 1.6 1000	NI 0.034 25	NI 0.61 440	NI 230 NI	NI 22 1000
β-Glucosidase Almond Caldocellum saccharolyticum	200 100	1000 230	NI NI	80 50	NI NI	NI 560
Trehalase Porcine kidney	41	5.6	NI	NI	NI	600

Table 3 Concentrations of glucosides of DNJ giving 50% inhibition of glycosidase activities(μM)

Enzymes	IC₅₀(μM)
	DNJ	11	14	16	12	15
	R₁=H, R₂=H, R₃=H^a	R₁=α-Glc, R₂=H, R₃=H	R₁=H, R₂=α-Glc, R₃=H	R₁=H, R₂=H, R₃=α-Glc	R₁=β-Glc, R₂=H, R₃=H	R₁=H, R₂=H, R₃=β-Glc
Rat intestinal maltose	0.36	24	5.2	2.3	4.0	24
Rat intestinal sucrose	0.21	2.4	0.35	0.4	0.79	2.5
Rat intestinal palatinose	0.3	6.2	0.9	0.47	1.4	2.7
Rat intestinal trehalose	42	2.2	NI	NI	NI	NI
Rat intestinal cellobiose	520	NI^b	NI	NI	NI	NI
Rat intestinal lactose	34	NI	NI	NI	520	460
α-Glucosidase Baker’s yeast Rice Rat liver lysosome	330 0.05 0.4	NI 1.6 1000	NI 0.034 25	NI 0.61 440	NI 230 NI	NI 22 1000
β-Glucosidase Almond Caldocellum saccharolyticum	200 100	1000 230	NI NI	80 50	NI NI	NI 560
Trehalase Porcine kidney	41	5.6	NI	NI	NI	600

Scheme. 3 Synthesis of the naturally occurring 6-O-α-D-galactopyranosyl-DNJ by enzymatic method[69]

Scheme. 4 Synthesis of galactosylated DNJ derivatives by enzymatic method[58]

Scheme. 5 Synthesis of 4-O-β-D-galactopyranosyl-DNJ by enzymatic method[59,60,61]

Scheme. 6 Synthesis of glucosylated DMDP derivatives by enzymatic method[68]

Scheme. 7 Synthesis of cello-oligomers of isofagomine and a tetrahydrooxazine with glycosynthases[62]

Scheme. 8 BhxE334G-catalyzed synthesis of xylanase inhibitors[65]

Table 4 Glycosides of iminosugars synthesized by chemical method and their biological activities

	Biological activities		Ref
	ND^a		54
	107: Maltase(yeast)-K_i-5.5 μM; Isomaltase(yeast)-K_i-55 μM Naringinase(P. decumbes)-K_i-702 μM^[70] 108: Maltase(yeast)-K_i-30 μM; Isomaltase(yeast)-K_i-52 μM Naringinase(P. decumbes)-K_i-187 μM^[70] 109: β-Glucosidase(bovine liver)-K_i- 195 μM; Maltase(yeast)-K_i-17 μM Isomaltase(yeast) -K_i-53 μM; Trehalase(pig kidney)-K_i-549 μM Naringinase(P. decumbes)-K_i-742 μM^[70]		70
	110: Maltase(yeast)-K_i-24 μM; Isomaltase(yeast)-K_i-36 μM Naringinase(P. decumbes)-K_i-160 μM^[70] 111: β-Glucosidase(almonds)-K_i- 209 μM^[70] 112: β-Glucosidase(bovine liver)-K_i- 190 μM; β-Glucosidase(almonds)-K_i- 375 μM; Maltase(yeast)-K_i-108 μM Isomaltase(yeast) -K_i-83 μM; Naringinase(P. decumbes)-K_i-443 μM^[70]		70
	R₁ R₂ R₃ R₄ - Inhibition of rat liver Golgi endomannosidase 113a OH OH OMe H - ND 113b OH OH H H - ND 113c OH OMe OH H - ND 113d OH H OH H - ND 113e OMe OH OH H - ND 113f H OH OH H - IC₅₀300 μM^[52] 113g OH OH OH Me - ND 113h OH OH OH n-propyl - ND		54
	R R₁ R₂ R₃ R₄ - Inhibition of rat liver Golgi endomannosidase 114a OMe OH OH H CH₂OH -IC₅₀4.4 μM^[52] 114b Cl OH OH H CH₂OH -IC₅₀17 μM^[52] 114c OH H OH H CH₂OH -IC₅₀390 μM^[52] 114d OH OH H H CH₂OH - ND 114e OH OH OMe H CH₂OH -ND 114f OH OH H OH CH₂OH -IC₅₀10 μM^[52] 114g OH OH OH H CH₃ -IC₅₀10 μM^[52] 114h OH OH OH H H -ND		71
	R R₁ R₂ - Inhibition of rat liver Golgi endomannosidase 115a H H H - IC₅₀28 μM^[52] 115b OH Me H - IC₅₀350 μM^[52] 115c OH H Me - IC₅₀400 μM^[52]		71
	R₁ R₂ R - Inhibition of endo-α-D-mannosidase 61 OH H H - IC₅₀5.6 μM^{[52, 72]} 116 H OH H - IC₅₀25.1 μM^[72] 117 H OH (CH₂)₅CN - ND 118 H OH (CH₂)₅NH₂ - ND		54, 72, 73
	BtGH99-K_d=97.7±4.9 μM^[74]		74
	ND		75
	Endo-β-1,4-(xylo)glucan hydrolase ( Paenibacillus polymyxa)-IC₅₀1.3 μM^[64] Cex(cellulomonas fimi)-K_i28 nM^[76] Cel5A( Bacillus agaradhaerens)-K_i26 nM^[76]		64, 76
	CtLic26 A(Clostridium thermocellum)-K_i168 nM^[76]		76
	BtGH99-K_d=0.03±0.01 μM^[77] BxGH99-K_d=0.013±0.002 μM^[77]		77
	See Table 2^[57]		78
	See Table 2^[57]		78
	124 R=Bu, β-Glucocerebrosidase-IC₅₀56 μM^[79] 125 R=H, β-Glucocerebrosidase-NI^[79]		79
R₁ R₂ 126 OH H - NKR-P1A IC₅₀5.5 μM^[80], CD69 IC₅₀3.3 μM^[80] 127 H OH - NKR-P1A IC₅₀6.5 μM^[80], CD69 IC₅₀4.5 μM^[80]		80
	R₁ R₂ 128 OH H -ND 129 H OH -ND		81
	Cel7A -K_i- 40 μM, Cel6A-K_i- 700 μM^[82]		82
	Cel7A -K_i- 1300 μM, Cel6A-K_i- 300 μM^[82]		82
	Cel7A -K_i- 190 μM, Cel6A-K_i- 5 μM^[82]		82
	Cel7A -K_i- 740 μM, Cel6A-K_i- 1 μM^[82]		82
	Cel7A -K_i- 6000 μM, Cel6A-K_i- 14 μM^[82]		82
	Cel7A -K_i- 130 μM, Cel6A-K_i- 1 μM^[82]		82
	ND		74
	Cel7A -K_i- 1000 μM, Cel6A-K_i- 130 μM^[82]		82, 83
	No inhibition at 2 mM^[82]		82
	Cel7A-IC₅₀4 mM^[84]		84
	Weak inhibitor of Cel7A^[84]		84
	ND		85
	ND		85
	ND		85
	Potent inhibitory effect on the adhesion of fixed HL-60 cells to IL-β-stimulated HUVECs, potency: N-butyl > N-decyl > N-methyl derivative.^[86]		86, 87
	Potent inhibitory effect on the adhesion of fixed HL-60 cells to IL-β-stimulated HUVECs, potency: N-butyl > N-decyl > N-methyl derivative. The sLe^a-type analogs(153~156) expressed stronger activity than the corresponding sLe^x-type analogs(149~152).^[86]		86
	No antibacterial activity detected^[88]		88
	No antibacterial activity detected^[88]		88
	Potential anti-diabetic effects^[78]		78, 89
	ND		87
	Potent inhibitory effect on the adhesion of fixed HL-60 cells to IL-β-stimulated HUVECs. The sulfo Le^a-type analogs(161~163) expressed stronger activity than the corresponding sulfo Le^x-type analogs(164~166).^[86]		86, 90
	Potent inhibitory effect on the adhesion of fixed HL-60 cells to IL-β-stimulated HUVECs.^[86]		86
	Potential anti-diabetic effects^[91]		91
	Potential anti-diabetic effects^[91]		91
	Show anti-inflammatory activity and retain the biological activity of the parent PIM structures^[92]		92
	The introduction of a functionalized spacer of the acylaminocaproyl type onto the piperidine ring of the PIM₂ mimic does not alter the immuno-modulating activity of the parent compound. This conjugate binds to macrophage membranes with rapid kinetics, and does not exhibit cytotoxicity while retaining the ability to inhibit LPS-induced production of proin?ammatory cytokines such as TNFα and IL12p40.^[93]		93
	Signi?cant cytotoxicity^[93]		93
	ND		94
	Barley 1,3-β-D-glucan endo-hydrolase-ID₅₀ 7.8 μM^[95] Potent inhibitor of bacterial endo-α-mannosidase^[96]		95, 96
	BtGH99-K_d=140 nM^[97] BxGH99-K_d=217 nM^[97]		97
	Barley 1,3-β-D-glucan endo-hydrolase-ID₅₀ 3.1 μM^[95]		95
	Heparanase(melanoma)-IC₅₀140 μM^[98] Heparanase(colon 26 N-17 cells)-IC₅₀58-63 μM^[98]		98
	ND		99
	ND		100
	ND		101
	ND		101
	Xylanase Cex(Cellulomonas fimi)-K_i- 0.15 μM^[66] Xylanase Bcx(Bacillus circulans)-K_i- 520 μM^[66]		66
	Xylanase Cex(Cellulomonas fimi)-K_i- 0.37 μM^[66] Xylanase Bcx(Bacillus circulans)-K_i- 1400 μM^[66]		66
	Xylanase Cex(Cellulomonas fimi)-K_i- 5.8 μM^[66] Xylanase Bcx(Bacillus circulans)-K_i- 1500 μM^[66]		66
	Xylanase Cex(Cellulomonas fimi)-K_i- 0.13 μM^[66] Xylanase Bcx(Bacillus circulans)-K_i- 1100 μM^[66]		66
	Xylanase Cex(Cellulomonas fimi)-K_i- 190 μM^[66] Xylanase Bcx(Bacillus circulans)-NI^[66]		66
	Xylanase Cex(Cellulomonas fimi)-K_i- 110 μM^[66] Xylanase Bcx(Bacillus circulans)-K_i- 3100 μM^[66]		66
	Xylanase Cex(Cellulomonas fimi)-K_i- 790 μM^[66] Xylanase Bcx(Bacillus circulans)-NI^[66]		66
	Wild-type Cex xylanase-K_i- 0.33 μM^[102]		102
	ND		103
	ND		103
	ND		103
	ND		103
	ND		103
	ND		104
	Transglycosylase(Acinetobacter baumannii): 70% inhibition at 50 μM^[105]		105
	NI^{b[106, 107]}		106, 107
	NI^{[106, 107]}		106, 107
	Rat intestinal sucrase-IC₅₀ 0.2 μM^[108] Rat intestinal maltase-IC₅₀ 1.0 μM^[108] Rat intestinal isomaltase-IC₅₀ 8.0 μM^[108] Glucoamylase-IC₅₀ 5.0 μM^[108]		108
	α-Glucosidase(yeast)-IC₅₀ 175 μM^[109]		109
	α-Glucosidase(yeast)-IC₅₀ 940 μM^[109]		109
	α-Glucosidase(yeast)-IC₅₀ 53 μM^[109]		109
	α-Glucosidase(yeast)-IC₅₀ 340 μM^[109]		109
	α-Glucosidase(yeast)-IC₅₀ 2400 μM^[109]		109
	α-Glucosidase(yeast)-IC₅₀ 1020 μM^[109]		109
	α-Glucosidase(yeast)-K_i- 59±2 μM^[110] β-Glucosidase(sweet almonds)-K_i- 2.3±0.4 μM^[110] Isomaltase(yeast) -K_i- 100±10 μM^[110] Glucoamylase(Aspergillus awamori)-K_i- 0.063±0.003 μM^[110]		110
	α-Glucosidase(yeast)-K_i- 70±8 μM^[110] β-Glucosidase(sweet almonds)-K_i- 0.38±0.02 μM^[110] Isomaltase(yeast) -K_i- 19±2 μM^[110] Glucoamylase(Aspergillus awamori)-K_i- 0.24±0.04 μM^[110]		110
	α-Glucosidase(yeast)-K_i- 280±60 μM^[110] β-Glucosidase(sweet almonds)-K_i- 150±10 μM^[110] Isomaltase(yeast)-K_i > 1000 μM^[110] Glucoamylase(Aspergillus awamori)-K_i- 94±10 μM^[110]		110
	α-Glucosidase(yeast)-K_i > 1000 μM^[110] β-Glucosidase(sweet almonds)-K_i- 510±30 μM^[110] Isomaltase(yeast)-K_i-190±20 μM^[110] Glucoamylase(Aspergillus awamori)-K_i- 160±20 μM^[110]		110
	223: α-1,3-Fucosyltransferase IV-IC₅₀ > 500 μM^[111] 224: α-1,3-Fucosyltransferase IV-IC₅₀-233 μM^[111]		111
	225: α-1,3-Fucosyltransferase IV-IC₅₀-81 μM^[111]		111
	226: IVT IC₅₀-5.7 μM, RNA IC₅₀-11 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus)-64 μg/mL^[112] 227: IVT IC₅₀-110 μM, RNA IC₅₀> 250 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus) > 64 μg/mL^[112] 228: IVT IC₅₀-75 μM, RNA IC₅₀> 250 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus) > 64 μg/mL^[112] 229: IVT IC₅₀-82 μM, RNA IC₅₀> 250 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus) > 64 μg/mL^[112] 230: IVT IC₅₀-36 μM, RNA IC₅₀> 250 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus) > 64 μg/mL^[112] 231: IVT IC₅₀-75 μM, RNA IC₅₀> 250 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus) > 64 μg/mL^[112] 232: IVT IC₅₀> 1000 μM, RNA IC₅₀> 250 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus) > 64 μg/mL^[112]		112
	233: IVT IC₅₀> 1000 μM, RNA IC₅₀> 250 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus) > 64 μg/mL^[112]		112
	234: IVT IC₅₀-6.4 μM, RNA IC₅₀-12 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus)-32 μg/mL^[112] 235: IVT IC₅₀-180 μM, RNA IC₅₀-80 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus) > 64 μg/mL^[112]		112
	236: IVT IC₅₀-39 μM, RNA IC₅₀> 250 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus) > 64 μg/mL^[112] 237: IVT IC₅₀-370 μM, RNA IC₅₀> 250 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus) > 64 μg/mL^[112]		112
	238: IVT IC₅₀-47 μM, RNA IC₅₀> 250 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus) > 64 μg/mL^[112] 239: IVT IC₅₀-230 μM, RNA IC₅₀> 250 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus) > 64 μg/mL^[112]		112
	No inhibition at a concentration of 500 μM towards human heparanase^[113]		113
	No inhibition at a concentration of 500 μM towards human heparanase^[113]		113
	No inhibition at a concentration of 500 μM towards human heparanase^[113]		113
	No inhibition at a concentration of 500 μM towards human heparanase^[113]		113
	244: C. riparius trehalase-IC₅₀9.36±1.49 μM^[114] Porcine trehalase-IC₅₀27.64±5.35 μM^[114] 245: C. riparius trehalase-IC₅₀>1000 μM^[114] Porcine trehalase-ND 246: C. riparius trehalase-IC₅₀>1000 μM^[114] Porcine trehalase-ND		114
	247: C. riparius trehalase-IC₅₀0.784±0.059 μM^[114] Porcine trehalase-IC₅₀5.84±0.26 μM^[114]		114
	ND		115
	Inhibits the binding of SLe^x glycoconjugate to immobilized recombinant(E)-selectin with IC₅₀ as 10 mM.^[116]		116
	Compound 251 is resistant to α-fucosidase and β-galactosidase and is active as inhibitor of SLe^x glycoconjugate binding to immobilized(E)-selectin with IC₅₀ as 10 mM.^[117]		117
	ND		118
	Devoid of E-selectin binding activity-IC₅₀> 10 μM^[119]		119
	254: α-Glucosidase(yeast)-K_i > 0.6 mM^[120] β-Glucosidase(almonds)-K_i- 3.18 mM^[120] 255: α-Glucosidase(yeast)-K_i > 1.38 mM^[120] β-Glucosidase(almonds)-K_i- 6.89 mM^[120] 256: α-Glucosidase(yeast)-K_i > 2.05 mM^[120] β-Glucosidase(almonds)-NI^[120]		120
	α-Glucosidase(yeast)-K_i > 0.96 mM^[120] β-Glucosidase(almonds)-K_i- 0.58 mM^[120]		120
	ND		121
	ND		121
	ND		121
	Mtb GlgE-K_i=237±27 μM^[122] GlgEI-K_i=102±7.52 μM^[122]		122
	262: GlgEI-K_i=45±4 μM^[123] 263: GlgEI-K_i=95±16 μM^[123]		123
	Binding with plasma protein: K_D=8.95 nM(rats), 27.2 nM(monkeys)^[124] Binding wit salivary amylase K_D=5.64 nM^[124]		124, 125
	ND		126
	ND		126
	ND		126
	ND		126
	56: Porcine kidney trehalase -K_i- 11 nM^[127] Escherichia coli trehalase(Tre37 A) -K_i- 12 nM^[127] Chironomus riparius trehalase -K_i- 0.66 nM^[127] Aspergillus niger glucoamylase-IC₅₀ 4.4 μM^[17] 271: Porcine kidney trehalase -K_i > 10 μM^[127] Escherichia coli trehalase(Tre37 A) -K_i- 2.8 μM^[127] Chironomus riparius trehalase -K_i- 157 nM^[127] Aspergillus niger glucoamylase-IC₅₀ 23.7 μM^[17] 272: Porcine kidney trehalase -K_i- 138 nM^[127] Escherichia coli trehalase(Tre37 A) -K_i- 86 nM^[127] Chironomus riparius trehalase -K_i- 22 nM^[127] Aspergillus niger glucoamylase-IC₅₀ 7.7 μM^[17]		17, 127
	C. riparius trehalase-IC₅₀29.49±7.26 μM^[114] Porcinetrehalase-IC₅₀190.60±34.15 μM^[114]		114
	Aspergillus niger glucoamylase(percentage inhibition at 1 mM concentration) 274: 0^[17] 275: 25%^[17] 276: 76%^[17]		17
	The alkaloids can trigger type 1 immune response of antigens, induce the production of IL-2 in dendritic cells, and was also found with anti-HIV activity.^{[128,129,130]}		131
	The alkaloids can trigger type 1 immune response of antigens, induce the production of IL-2 in dendritic cells, and was also found with anti-HIV activity.^{[128,129,130]}		131
	The alkaloids can trigger type 1 immune response of antigens, induce the production of IL-2 in dendritic cells, and was also found with anti-HIV activity.^{[128,129,130]}		131
	ND		132
	Human recombinant endo-α-mannosidase(up to 1 mM concentration)-NI^[133] No binding to either the wild-type or E154 A variant(vide infra) BtGH99^[133]		133
	Devoid of E-selectin binding activity-IC₅₀> 10 μM^[119]		119
	E-selectin: No affinity^[119] P-selectin: In low μM range^[119]		119
	E-selectin: No affinity^[119] P-selectin: In low μM range^[119]		119
	E-selectin: No affinity^[119] P-selectin: In low μM range^[119]		119
	ND		134
	291: Rat intestinal sucrase-IC₅₀ 0.04 μM^[19] Lysosomal α-glucosidase-IC₅₀ 40 μM^[19] 292: Rat intestinal sucrase-IC₅₀ 0.03 μM^[19] Lysosomal α-glucosidase-IC₅₀ 40 μM^[19] 58: Rat intestinal sucrase-IC₅₀ 0.4 μM^[19] Lysosomal α-glucosidase-IC₅₀ > 400 μM^[19]		19, 134

Table 4 Glycosides of iminosugars synthesized by chemical method and their biological activities

	Biological activities		Ref
	ND^a		54
	107: Maltase(yeast)-K_i-5.5 μM; Isomaltase(yeast)-K_i-55 μM Naringinase(P. decumbes)-K_i-702 μM^[70] 108: Maltase(yeast)-K_i-30 μM; Isomaltase(yeast)-K_i-52 μM Naringinase(P. decumbes)-K_i-187 μM^[70] 109: β-Glucosidase(bovine liver)-K_i- 195 μM; Maltase(yeast)-K_i-17 μM Isomaltase(yeast) -K_i-53 μM; Trehalase(pig kidney)-K_i-549 μM Naringinase(P. decumbes)-K_i-742 μM^[70]		70
	110: Maltase(yeast)-K_i-24 μM; Isomaltase(yeast)-K_i-36 μM Naringinase(P. decumbes)-K_i-160 μM^[70] 111: β-Glucosidase(almonds)-K_i- 209 μM^[70] 112: β-Glucosidase(bovine liver)-K_i- 190 μM; β-Glucosidase(almonds)-K_i- 375 μM; Maltase(yeast)-K_i-108 μM Isomaltase(yeast) -K_i-83 μM; Naringinase(P. decumbes)-K_i-443 μM^[70]		70
	R₁ R₂ R₃ R₄ - Inhibition of rat liver Golgi endomannosidase 113a OH OH OMe H - ND 113b OH OH H H - ND 113c OH OMe OH H - ND 113d OH H OH H - ND 113e OMe OH OH H - ND 113f H OH OH H - IC₅₀300 μM^[52] 113g OH OH OH Me - ND 113h OH OH OH n-propyl - ND		54
	R R₁ R₂ R₃ R₄ - Inhibition of rat liver Golgi endomannosidase 114a OMe OH OH H CH₂OH -IC₅₀4.4 μM^[52] 114b Cl OH OH H CH₂OH -IC₅₀17 μM^[52] 114c OH H OH H CH₂OH -IC₅₀390 μM^[52] 114d OH OH H H CH₂OH - ND 114e OH OH OMe H CH₂OH -ND 114f OH OH H OH CH₂OH -IC₅₀10 μM^[52] 114g OH OH OH H CH₃ -IC₅₀10 μM^[52] 114h OH OH OH H H -ND		71
	R R₁ R₂ - Inhibition of rat liver Golgi endomannosidase 115a H H H - IC₅₀28 μM^[52] 115b OH Me H - IC₅₀350 μM^[52] 115c OH H Me - IC₅₀400 μM^[52]		71
	R₁ R₂ R - Inhibition of endo-α-D-mannosidase 61 OH H H - IC₅₀5.6 μM^{[52, 72]} 116 H OH H - IC₅₀25.1 μM^[72] 117 H OH (CH₂)₅CN - ND 118 H OH (CH₂)₅NH₂ - ND		54, 72, 73
	BtGH99-K_d=97.7±4.9 μM^[74]		74
	ND		75
	Endo-β-1,4-(xylo)glucan hydrolase ( Paenibacillus polymyxa)-IC₅₀1.3 μM^[64] Cex(cellulomonas fimi)-K_i28 nM^[76] Cel5A( Bacillus agaradhaerens)-K_i26 nM^[76]		64, 76
	CtLic26 A(Clostridium thermocellum)-K_i168 nM^[76]		76
	BtGH99-K_d=0.03±0.01 μM^[77] BxGH99-K_d=0.013±0.002 μM^[77]		77
	See Table 2^[57]		78
	See Table 2^[57]		78
	124 R=Bu, β-Glucocerebrosidase-IC₅₀56 μM^[79] 125 R=H, β-Glucocerebrosidase-NI^[79]		79
R₁ R₂ 126 OH H - NKR-P1A IC₅₀5.5 μM^[80], CD69 IC₅₀3.3 μM^[80] 127 H OH - NKR-P1A IC₅₀6.5 μM^[80], CD69 IC₅₀4.5 μM^[80]		80
	R₁ R₂ 128 OH H -ND 129 H OH -ND		81
	Cel7A -K_i- 40 μM, Cel6A-K_i- 700 μM^[82]		82
	Cel7A -K_i- 1300 μM, Cel6A-K_i- 300 μM^[82]		82
	Cel7A -K_i- 190 μM, Cel6A-K_i- 5 μM^[82]		82
	Cel7A -K_i- 740 μM, Cel6A-K_i- 1 μM^[82]		82
	Cel7A -K_i- 6000 μM, Cel6A-K_i- 14 μM^[82]		82
	Cel7A -K_i- 130 μM, Cel6A-K_i- 1 μM^[82]		82
	ND		74
	Cel7A -K_i- 1000 μM, Cel6A-K_i- 130 μM^[82]		82, 83
	No inhibition at 2 mM^[82]		82
	Cel7A-IC₅₀4 mM^[84]		84
	Weak inhibitor of Cel7A^[84]		84
	ND		85
	ND		85
	ND		85
	Potent inhibitory effect on the adhesion of fixed HL-60 cells to IL-β-stimulated HUVECs, potency: N-butyl > N-decyl > N-methyl derivative.^[86]		86, 87
	Potent inhibitory effect on the adhesion of fixed HL-60 cells to IL-β-stimulated HUVECs, potency: N-butyl > N-decyl > N-methyl derivative. The sLe^a-type analogs(153~156) expressed stronger activity than the corresponding sLe^x-type analogs(149~152).^[86]		86
	No antibacterial activity detected^[88]		88
	No antibacterial activity detected^[88]		88
	Potential anti-diabetic effects^[78]		78, 89
	ND		87
	Potent inhibitory effect on the adhesion of fixed HL-60 cells to IL-β-stimulated HUVECs. The sulfo Le^a-type analogs(161~163) expressed stronger activity than the corresponding sulfo Le^x-type analogs(164~166).^[86]		86, 90
	Potent inhibitory effect on the adhesion of fixed HL-60 cells to IL-β-stimulated HUVECs.^[86]		86
	Potential anti-diabetic effects^[91]		91
	Potential anti-diabetic effects^[91]		91
	Show anti-inflammatory activity and retain the biological activity of the parent PIM structures^[92]		92
	The introduction of a functionalized spacer of the acylaminocaproyl type onto the piperidine ring of the PIM₂ mimic does not alter the immuno-modulating activity of the parent compound. This conjugate binds to macrophage membranes with rapid kinetics, and does not exhibit cytotoxicity while retaining the ability to inhibit LPS-induced production of proin?ammatory cytokines such as TNFα and IL12p40.^[93]		93
	Signi?cant cytotoxicity^[93]		93
	ND		94
	Barley 1,3-β-D-glucan endo-hydrolase-ID₅₀ 7.8 μM^[95] Potent inhibitor of bacterial endo-α-mannosidase^[96]		95, 96
	BtGH99-K_d=140 nM^[97] BxGH99-K_d=217 nM^[97]		97
	Barley 1,3-β-D-glucan endo-hydrolase-ID₅₀ 3.1 μM^[95]		95
	Heparanase(melanoma)-IC₅₀140 μM^[98] Heparanase(colon 26 N-17 cells)-IC₅₀58-63 μM^[98]		98
	ND		99
	ND		100
	ND		101
	ND		101
	Xylanase Cex(Cellulomonas fimi)-K_i- 0.15 μM^[66] Xylanase Bcx(Bacillus circulans)-K_i- 520 μM^[66]		66
	Xylanase Cex(Cellulomonas fimi)-K_i- 0.37 μM^[66] Xylanase Bcx(Bacillus circulans)-K_i- 1400 μM^[66]		66
	Xylanase Cex(Cellulomonas fimi)-K_i- 5.8 μM^[66] Xylanase Bcx(Bacillus circulans)-K_i- 1500 μM^[66]		66
	Xylanase Cex(Cellulomonas fimi)-K_i- 0.13 μM^[66] Xylanase Bcx(Bacillus circulans)-K_i- 1100 μM^[66]		66
	Xylanase Cex(Cellulomonas fimi)-K_i- 190 μM^[66] Xylanase Bcx(Bacillus circulans)-NI^[66]		66
	Xylanase Cex(Cellulomonas fimi)-K_i- 110 μM^[66] Xylanase Bcx(Bacillus circulans)-K_i- 3100 μM^[66]		66
	Xylanase Cex(Cellulomonas fimi)-K_i- 790 μM^[66] Xylanase Bcx(Bacillus circulans)-NI^[66]		66
	Wild-type Cex xylanase-K_i- 0.33 μM^[102]		102
	ND		103
	ND		103
	ND		103
	ND		103
	ND		103
	ND		104
	Transglycosylase(Acinetobacter baumannii): 70% inhibition at 50 μM^[105]		105
	NI^{b[106, 107]}		106, 107
	NI^{[106, 107]}		106, 107
	Rat intestinal sucrase-IC₅₀ 0.2 μM^[108] Rat intestinal maltase-IC₅₀ 1.0 μM^[108] Rat intestinal isomaltase-IC₅₀ 8.0 μM^[108] Glucoamylase-IC₅₀ 5.0 μM^[108]		108
	α-Glucosidase(yeast)-IC₅₀ 175 μM^[109]		109
	α-Glucosidase(yeast)-IC₅₀ 940 μM^[109]		109
	α-Glucosidase(yeast)-IC₅₀ 53 μM^[109]		109
	α-Glucosidase(yeast)-IC₅₀ 340 μM^[109]		109
	α-Glucosidase(yeast)-IC₅₀ 2400 μM^[109]		109
	α-Glucosidase(yeast)-IC₅₀ 1020 μM^[109]		109
	α-Glucosidase(yeast)-K_i- 59±2 μM^[110] β-Glucosidase(sweet almonds)-K_i- 2.3±0.4 μM^[110] Isomaltase(yeast) -K_i- 100±10 μM^[110] Glucoamylase(Aspergillus awamori)-K_i- 0.063±0.003 μM^[110]		110
	α-Glucosidase(yeast)-K_i- 70±8 μM^[110] β-Glucosidase(sweet almonds)-K_i- 0.38±0.02 μM^[110] Isomaltase(yeast) -K_i- 19±2 μM^[110] Glucoamylase(Aspergillus awamori)-K_i- 0.24±0.04 μM^[110]		110
	α-Glucosidase(yeast)-K_i- 280±60 μM^[110] β-Glucosidase(sweet almonds)-K_i- 150±10 μM^[110] Isomaltase(yeast)-K_i > 1000 μM^[110] Glucoamylase(Aspergillus awamori)-K_i- 94±10 μM^[110]		110
	α-Glucosidase(yeast)-K_i > 1000 μM^[110] β-Glucosidase(sweet almonds)-K_i- 510±30 μM^[110] Isomaltase(yeast)-K_i-190±20 μM^[110] Glucoamylase(Aspergillus awamori)-K_i- 160±20 μM^[110]		110
	223: α-1,3-Fucosyltransferase IV-IC₅₀ > 500 μM^[111] 224: α-1,3-Fucosyltransferase IV-IC₅₀-233 μM^[111]		111
	225: α-1,3-Fucosyltransferase IV-IC₅₀-81 μM^[111]		111
	226: IVT IC₅₀-5.7 μM, RNA IC₅₀-11 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus)-64 μg/mL^[112] 227: IVT IC₅₀-110 μM, RNA IC₅₀> 250 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus) > 64 μg/mL^[112] 228: IVT IC₅₀-75 μM, RNA IC₅₀> 250 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus) > 64 μg/mL^[112] 229: IVT IC₅₀-82 μM, RNA IC₅₀> 250 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus) > 64 μg/mL^[112] 230: IVT IC₅₀-36 μM, RNA IC₅₀> 250 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus) > 64 μg/mL^[112] 231: IVT IC₅₀-75 μM, RNA IC₅₀> 250 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus) > 64 μg/mL^[112] 232: IVT IC₅₀> 1000 μM, RNA IC₅₀> 250 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus) > 64 μg/mL^[112]		112
	233: IVT IC₅₀> 1000 μM, RNA IC₅₀> 250 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus) > 64 μg/mL^[112]		112
	234: IVT IC₅₀-6.4 μM, RNA IC₅₀-12 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus)-32 μg/mL^[112] 235: IVT IC₅₀-180 μM, RNA IC₅₀-80 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus) > 64 μg/mL^[112]		112
	236: IVT IC₅₀-39 μM, RNA IC₅₀> 250 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus) > 64 μg/mL^[112] 237: IVT IC₅₀-370 μM, RNA IC₅₀> 250 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus) > 64 μg/mL^[112]		112
	238: IVT IC₅₀-47 μM, RNA IC₅₀> 250 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus) > 64 μg/mL^[112] 239: IVT IC₅₀-230 μM, RNA IC₅₀> 250 μM, MIC(E. coli) > 64 μg/mL, MIC(S. aureus) > 64 μg/mL^[112]		112
	No inhibition at a concentration of 500 μM towards human heparanase^[113]		113
	No inhibition at a concentration of 500 μM towards human heparanase^[113]		113
	No inhibition at a concentration of 500 μM towards human heparanase^[113]		113
	No inhibition at a concentration of 500 μM towards human heparanase^[113]		113
	244: C. riparius trehalase-IC₅₀9.36±1.49 μM^[114] Porcine trehalase-IC₅₀27.64±5.35 μM^[114] 245: C. riparius trehalase-IC₅₀>1000 μM^[114] Porcine trehalase-ND 246: C. riparius trehalase-IC₅₀>1000 μM^[114] Porcine trehalase-ND		114
	247: C. riparius trehalase-IC₅₀0.784±0.059 μM^[114] Porcine trehalase-IC₅₀5.84±0.26 μM^[114]		114
	ND		115
	Inhibits the binding of SLe^x glycoconjugate to immobilized recombinant(E)-selectin with IC₅₀ as 10 mM.^[116]		116
	Compound 251 is resistant to α-fucosidase and β-galactosidase and is active as inhibitor of SLe^x glycoconjugate binding to immobilized(E)-selectin with IC₅₀ as 10 mM.^[117]		117
	ND		118
	Devoid of E-selectin binding activity-IC₅₀> 10 μM^[119]		119
	254: α-Glucosidase(yeast)-K_i > 0.6 mM^[120] β-Glucosidase(almonds)-K_i- 3.18 mM^[120] 255: α-Glucosidase(yeast)-K_i > 1.38 mM^[120] β-Glucosidase(almonds)-K_i- 6.89 mM^[120] 256: α-Glucosidase(yeast)-K_i > 2.05 mM^[120] β-Glucosidase(almonds)-NI^[120]		120
	α-Glucosidase(yeast)-K_i > 0.96 mM^[120] β-Glucosidase(almonds)-K_i- 0.58 mM^[120]		120
	ND		121
	ND		121
	ND		121
	Mtb GlgE-K_i=237±27 μM^[122] GlgEI-K_i=102±7.52 μM^[122]		122
	262: GlgEI-K_i=45±4 μM^[123] 263: GlgEI-K_i=95±16 μM^[123]		123
	Binding with plasma protein: K_D=8.95 nM(rats), 27.2 nM(monkeys)^[124] Binding wit salivary amylase K_D=5.64 nM^[124]		124, 125
	ND		126
	ND		126
	ND		126
	ND		126
	56: Porcine kidney trehalase -K_i- 11 nM^[127] Escherichia coli trehalase(Tre37 A) -K_i- 12 nM^[127] Chironomus riparius trehalase -K_i- 0.66 nM^[127] Aspergillus niger glucoamylase-IC₅₀ 4.4 μM^[17] 271: Porcine kidney trehalase -K_i > 10 μM^[127] Escherichia coli trehalase(Tre37 A) -K_i- 2.8 μM^[127] Chironomus riparius trehalase -K_i- 157 nM^[127] Aspergillus niger glucoamylase-IC₅₀ 23.7 μM^[17] 272: Porcine kidney trehalase -K_i- 138 nM^[127] Escherichia coli trehalase(Tre37 A) -K_i- 86 nM^[127] Chironomus riparius trehalase -K_i- 22 nM^[127] Aspergillus niger glucoamylase-IC₅₀ 7.7 μM^[17]		17, 127
	C. riparius trehalase-IC₅₀29.49±7.26 μM^[114] Porcinetrehalase-IC₅₀190.60±34.15 μM^[114]		114
	Aspergillus niger glucoamylase(percentage inhibition at 1 mM concentration) 274: 0^[17] 275: 25%^[17] 276: 76%^[17]		17
	The alkaloids can trigger type 1 immune response of antigens, induce the production of IL-2 in dendritic cells, and was also found with anti-HIV activity.^{[128,129,130]}		131
	The alkaloids can trigger type 1 immune response of antigens, induce the production of IL-2 in dendritic cells, and was also found with anti-HIV activity.^{[128,129,130]}		131
	The alkaloids can trigger type 1 immune response of antigens, induce the production of IL-2 in dendritic cells, and was also found with anti-HIV activity.^{[128,129,130]}		131
	ND		132
	Human recombinant endo-α-mannosidase(up to 1 mM concentration)-NI^[133] No binding to either the wild-type or E154 A variant(vide infra) BtGH99^[133]		133
	Devoid of E-selectin binding activity-IC₅₀> 10 μM^[119]		119
	E-selectin: No affinity^[119] P-selectin: In low μM range^[119]		119
	E-selectin: No affinity^[119] P-selectin: In low μM range^[119]		119
	E-selectin: No affinity^[119] P-selectin: In low μM range^[119]		119
	ND		134
	291: Rat intestinal sucrase-IC₅₀ 0.04 μM^[19] Lysosomal α-glucosidase-IC₅₀ 40 μM^[19] 292: Rat intestinal sucrase-IC₅₀ 0.03 μM^[19] Lysosomal α-glucosidase-IC₅₀ 40 μM^[19] 58: Rat intestinal sucrase-IC₅₀ 0.4 μM^[19] Lysosomal α-glucosidase-IC₅₀ > 400 μM^[19]		19, 134

Scheme. 9 Synthesis of 3-O-α-D-Glucopyranosyl-DMJ and its derivatives with modified iminosugar ring[54]

Scheme. 10 Synthesis of glycosylated Sialyl Lewis X derivatives[118]

Scheme. 11 Synthesis of glycosylated iminosugars with fluorinated iminosugars as glycosyl donors[70]

Scheme. 12 Synthesis of glycosylated swainsonine derivatives[133]

Scheme. 13 Synthesis of glycosylated DNJ derivatives[137]

Scheme. 14 Synthesis of glycosylated casuarine derivatives[127, 138]

Scheme. 15 Synthesis of glycosylated castanospermine derivatives[134]

Scheme. 16 Synthesis of glycosylated isofagomine derivatives[95]

Fig. 3 Glycosylated polyhydroxylated pyrrolidines derivatives[125, 140]

Scheme. 17 Synthesis of glycosylated iminosugar mimetics of sialyl Lewis X[119]

Scheme. 18 Synthesis of diglycosylated DNJ derivatives[87]

Scheme. 19 Synthesis of glycosylated azepane derivatives[112]

Scheme. 20 Synthesis of glycosylated iminosugars with iminosugar thioglycosides as glycosyl donors[144]

Scheme. 21 Synthesis of glycosylated australine derivatives[132]

Scheme. 22 Synthesis of glycosylated iminosugar derivatives with stereoelectronical 1,2-shift as key step[121]

Scheme. 23 Synthesis of galactosylated DNJ from lactose[146]

Scheme. 24 Synthesis of glycosylated DMJ from maltulose[73]

Scheme. 25 Synthesis of glycosylated DNJ derivatives from maltose and cellose[147]

Scheme. 26 Synthesis of glucosylated DNJ derivatives from chitobiose[75]

Scheme. 27 Synthesis of mannosylated noeuromycin derivatives[77]

Scheme. 28 Synthesis of N-glycosylated DAB derivatives[115]

Scheme. 29 Synthesis of N-glycosylated isofagomine derivatives[110]

Scheme. 30 Synthesis of N-glycosylated DNJ and azepane[106, 107]

Scheme. 31 Synthesis of diglycosylated DNJ derivatives[91]

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Glycosylated Iminosugars: Isolation, Synthesis and Biological Activities

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Glycosylated Iminosugars: Isolation, Synthesis and Biological Activities