@article {doi:10.1021/acscentsci.5b00399,
	title = {Potent Human α-Amylase Inhibition by the β-Defensin-like Protein Helianthamide},
	journal = {ACS Central Science},
	volume = {2},
	number = {3},
	year = {2016},
	pages = {154-161},
	abstract = {Selective inhibitors of human pancreatic α-amylase (HPA) are an effective means of controlling blood sugar levels in the management of diabetes. A high-throughput screen of marine natural product extracts led to the identification of a potent (Ki = 10 pM) peptidic HPA inhibitor, helianthamide, from the Caribbean sea anemone Stichodactyla helianthus. Active helianthamide was produced in Escherichia coli via secretion as a barnase fusion protein. X-ray crystallographic analysis of the complex of helianthamide with porcine pancreatic α-amylase revealed that helianthamide adopts a β-defensin fold and binds into and across the amylase active site, utilizing a contiguous YIYH inhibitory motif. Helianthamide represents the first of a novel class of glycosidase inhibitors and provides an unusual example of functional malleability of the β-defensin fold, which is rarely seen outside of its traditional role in antimicrobial peptides.},
	doi = {10.1021/acscentsci.5b00399},
	url = {http://dx.doi.org/10.1021/acscentsci.5b00399},
	author = {Christina Tysoe and Leslie K. Williams and Robert Keyzers and Nham T. Nguyen and Chris Tarling and Jacqueline Wicki and Ethan D. Goddard-Borger and Adeleke H. Aguda and Suzanne Perry and Leonard J. Foster and Raymond J. Andersen and Gary D. Brayer and Stephen G. Withers}
}
