title: Conformationally restricted short peptides inhibit human islet amyloid polypeptide (hIAPP) fibrillization.
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.
authors: International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg, New Delhi 110067, India.
authors: Aseem
authors: A
authors: Mishra
authors: Anurag
authors: A
authors: Misra
authors: T Sri
authors: TS
authors: Vaishnavi
authors: Chaitanya
authors: C
authors: Thota
authors: Madhvi
authors: M
authors: Gupta
authors: Suryanarayanarao
authors: S
authors: Ramakumar
authors: Virander Singh
authors: VS
authors: Chauhan
mesh_terms: D018360:Crystallography, X-Ray; D006801:Humans; D058228:Islet Amyloid Polypeptide / Q000037:antagonists & inhibitors* / Q000737:chemistry; D008958:Models, Molecular; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D011487:Protein Conformation; D013329:Structure-Activity Relationship
chemical_list: D058228:Islet Amyloid Polypeptide; D010455:Peptides