@article {2280,
	title = {The search for novel human pancreatic alpha-amylase inhibitors: High-throughput screening of terrestrial and marine natural product extracts},
	journal = {Chembiochem},
	volume = {9},
	number = {3},
	year = {2008},
	note = {Tarling, Chris A. Woods, Kate Zhang, Ran Brastianos, Harry C. Brayer, Gary D. Andersen, Raymond J. Withers, Stephen G.},
	month = {Jan},
	pages = {433-438},
	abstract = {Specific inhibitors of human pancreatic a-amylase (HPA) have potential as oral agents for the control of blood glucose levels in the treatment of diabetes and obesity. In a search for novel inhibitors, a library of 30000 crude biological extracts of terrestrial and marine origin has been screened. A number of inhibitory extracts were identified, of which the most potent was subjected to 1 bioassay-guided purification. A family of three glycosylated acyl flavonols, montbretins A-C-1 was thereby identified and characterized as competitive amylase inhibitors, with K-i values ranging from 8.1-6100 nm. Competitive inhibition by myricetin, which corresponds to the flavone core, and noncompetitive inhibition by a second fragment, ethyl caffeiate, suggest a binding mode for these inhibitors.},
	isbn = {1439-4227},
	url = {<Go to ISI>://000253460000016},
	author = {Tarling, C. A. and Woods, K. and Zhang, R. and Brastianos, H. C. and Brayer, G. D. and Andersen, R. J. and Withers, S. G.}
}
