Conformationally restricted short peptides inhibit human islet amyloid polypeptide (hIAPP) fibrillization

Aseem Mishra; Anurag Misra; T Sri Vaishnavi; Chaitanya Thota; Madhvi Gupta; Suryanarayanarao Ramakumar; Virander Singh Chauhan

doi:10.1039/c3cc38982k

Conformationally restricted short peptides inhibit human islet amyloid polypeptide (hIAPP) fibrillization

Chem Commun (Camb). 2013 Apr 4;49(26):2688-90. doi: 10.1039/c3cc38982k.

Authors

Aseem Mishra¹, Anurag Misra, T Sri Vaishnavi, Chaitanya Thota, Madhvi Gupta, Suryanarayanarao Ramakumar, Virander Singh Chauhan

Affiliation

¹ International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg, New Delhi 110067, India.

Abstract

hIAPP fibrillization implicated in Type 2 diabetes pathology involves formation of oligomers toxic to insulin producing pancreatic β-cells. We report design, synthesis, 3D structure and functional characterization of dehydrophenylalanine (ΔF) containing peptides which inhibit hIAPP fibrillization. The inhibitor protects β-cells from hIAPP induced toxicity.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Crystallography, X-Ray
Humans
Islet Amyloid Polypeptide / antagonists & inhibitors*
Islet Amyloid Polypeptide / chemistry
Models, Molecular
Peptides / chemical synthesis
Peptides / chemistry
Peptides / pharmacology*
Protein Conformation
Structure-Activity Relationship

Substances

Islet Amyloid Polypeptide
Peptides