Alpha-glucosidase Inhibitors: Clinically Promising Candidates for Anti-diabetic Drug Discovery

Cover
Alpha-Glucosidase Inhibitors
Copyright
Quote from the Quran
Dedication
Contents
About the author
Preface
Acknowledgments
one Introduction, rationale and the current clinical status of oral α-glucosidase inhibitors
	1.1 Introduction
	1.2 Diabetes mellitus and the antidiabetic drugs
	1.3 α-Glucosidase inhibitors—past and present
	1.4 Rationale
	References
two Natural and synthetic sugar mimics
	2.1 Introduction
	2.2 Iminosugars
		2.2.1 Polyhydroxylated pyrrolidines
		2.2.2 Polyhydroxylated pyrrolizidines
		2.2.3 Polyhydroxylated quinolizidines
		2.2.4 Hydroxymethyl-branched polyhydroxylated indolizidines
		2.2.5 Nojirimycin derivatives
		2.2.6 Other derivatives
	2.3 Aminosugars
	2.4 Thiosugars
	2.5 Carbasugars
	References
three Polyphenols
	3.1 Chalcones
	3.2 Xanthones
	3.3 Flavonoids and other polyphenols
	References
four Terpenoids and steroids
	4.1 Terpenoids
	4.2 Steroid derivatives
	References
five Azoles and related derivatives
	5.1 Thiadiazoles, oxadiazoles, and triazoles
	5.2 Other related derivatives
		5.2.1 Oxindoles
		5.2.2 2-Arylquinazolin-4(3H)-one derivatives
		5.2.3 Bis-Indolylmethanes
		5.2.4 Metallophthalocyanines
		5.2.5 Thiobarbiturates
		5.2.6 Carbazoles and hydrazone-bridged thiazole-pyrrole derivatives
	References
six Cyclitols and miscellaneous inhibitors
	6.1 Cyclitols
	6.2 Polycyclitols
	6.3 Aminocyclitols
	6.4 Conduritols
	6.5 Inositols
	6.6 Miscellaneous derivatives
		6.6.1 Anthraquinones
		6.6.2 Sarcoviolins and terphenyl derivatives
		6.6.3 Stilbenes
		6.6.4 Stilbene-based urea derivatives
		6.6.5 Depsidones
		6.6.6 Macrolides
		6.6.7 Peptides
		6.6.8 Ganomycin I and its derivatives
		6.6.9 Carbenes
		6.6.10 Pyranoquinolinyl-acrylic acid diastereomers
		6.6.11 N,N′-bis-Cyanomethylamine and alkoxymethylamine derivatives
	References
seven Computational and structural biology of α-glucosidase-inhibitor complexes: clues to drug optimization and development
	7.1 Crystal structure of human MGAM-C in complex with acarbose
	7.2 Crystal structures of human MGAM-N in complex with acarbose, miglitol, and salacinol
	7.3 Comparison of the MGAM-N-inhibitor complexes
	7.4 The human MGAM-N-salacinol derivative complexes
	7.5 Comparison of the crystal structures of acarbose in complex with MGAM-C, MGAM-N, and SI-N
	7.6 Important structural and functional clues to human MGAM-N inhibition
	7.7 The human MAGAM-N-casuarine complex
	7.8 Crystal structures of free isomaltase and in complex with maltose
	7.9 Insights into the α-glucosidase mechanism of inhibition
	7.10 Computational simulations of α-glucosidase-inhibitor interactions
		7.10.1 The 3′-benzylated analog of 3′-epi-neoponkoranol
		7.10.2 Fluorescent DNJ derivatives
		7.10.3 The 5-arylidene-N,N-diethylthiobarbiturate derivatives
		7.10.4 The 3′-O-neopentyl derivative of salacinol
		7.10.5 Salvianolic acids C and A
		7.10.6 Pelargonidin-3-o-rutinoside and analogs
		7.10.7 Sericin peptide
	References
Appendix A comprehensive list of promising α-glucosidase inhibitors with the activity data discussed in the book
Index
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