These authors contributed equally to the work.
Synthetic α-Helix Mimetics as Agonists and Antagonists of Islet Amyloid Polypeptide Aggregation†
Article first published online: 22 DEC 2009
Copyright © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 49, Issue 4, pages 736–739, January 18, 2010
How to Cite
Saraogi, I., Hebda, James A., Becerril, J., Estroff, Lara A., Miranker, Andrew D. and Hamilton, Andrew D. (2010), Synthetic α-Helix Mimetics as Agonists and Antagonists of Islet Amyloid Polypeptide Aggregation. Angew. Chem. Int. Ed., 49: 736–739. doi: 10.1002/anie.200901694
We thank Prof. G. W. Brudvig for suggestions and Dr. C. Incarvito for assistance with X-ray crystallographic analysis. This work was supported by National Institutes of Health grants to A.D.H. (GM69850) and A.D.M. (NIDDK DK079829). J.A.H. was supported by a NRSA fellowship (AG031612).
- Issue published online: 13 JAN 2010
- Article first published online: 22 DEC 2009
- Manuscript Revised: 13 OCT 2009
- Manuscript Received: 28 MAR 2009
- National Institutes of Health. Grant Numbers: GM69850, NIDDK DK079829
- α-helix mimetics;
- amyloid β-peptides;
- helical structures;
Split personality: A series of oligoamide-based helix mimetics bind to a complementary helical motif in Islet amyloid polypeptide (IAPP), a protein implicated in the pathology of type II diabetes. These compounds accelerated IAPP amyloid formation under lipid-free conditions, but inhibited it under lipid-catalyzed conditions. hIAPP=human IAPP.