Volume 6 Supplement 1
Discovery of novel α-amylase inhibitors using structure-based drug design
© Al-Asri and Wolber; licensee Chemistry Central Ltd. 2014
Published: 11 March 2014
α-Amylase is an endoamylase and belongs to glycoside hydrolase family 13 (GH 13) according to the classification of carbohydrate-active enzymes . It initiates starch hydrolysis into smaller oligomers. Inhibitors of this enzyme are of pharmacological importance as α-amylase is considered as attractive target for treating elevated post-prandial blood glucose levels resulting in obesity and type II diabetes. Besides the application as a drug, it is highly interesting to classify nutritional components, such as food additives or secondary plant metabolites with respect to their modulation of α-amylase.
- Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, Henrissat B: The carbohydrate-active enzymes database (cazy): An expert resource for glycogenomics. Nucleic Acids Res. 2009, 37: D233-D238. 10.1093/nar/gkn663.View ArticleGoogle Scholar
- Qin X, Ren L, Yang X, Bai F, Wang L, Geng P, Bai G, Shen Y: Structures of human pancreatic alpha-amylase in complex with acarviostatins: Implications for drug design against type II diabetes. J Struct Biol. 2011, 174 (1): 196-202. 10.1016/j.jsb.2010.11.020.View ArticleGoogle Scholar
- Wolber G, Langer T: Ligandscout: 3-d pharmacophores derived from protein-bound ligands and their use as virtual screening filters. J Chem Inf Model. 2005, 45 (1): 160-169. 10.1021/ci049885e.View ArticleGoogle Scholar
This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.