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The Inhibition Pathways of Human Islet Amyloid Polypeptide
EP31018
Poster Title: The Inhibition Pathways of Human Islet Amyloid Polypeptide
Submitted on 22 Nov 2019
Author(s): Yuko P. Y. Lam1; Cookson K.C. Chiu1; Christopher A. Wootton1; Ji-Inn Song1; Meng Li1; Ian Hands-Portman2; Mark P. Barrow1; and Peter B. O'Connor1
Affiliations: 1 Department of Chemistry, University of Warwick, Coventry, UK 2 School of Life Science, University of Warwick, Coventry, UK
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Abstract: Human islet amyloid polypeptide (hIAPP) is a highly amyloidogenic protein

Amyloid proteins are inherently disordered with high conformation flexibility 1-2

Classic structure-based design for therapeutics drug development against amyloid proteins is challenging 3

Herein, mass spectrometry was used to identify binding regions of a range of reported hIAPP aggregation inhibitors, including human
insulin, (-)-Epigallocatechin 3-gallate (EGCG), 3-amino-1-propane sulfonic acid (3-APS), and 1H-Benzimidazole-2-sulfonic acid (BISA)

Deamidated hIAPP accelerates amyloid fibril formation,4 but the interactions with reported aggregation inhibitors are unknown
Summary: Human islet amyloid polypeptide (hIAPP) is a highly amyloidogenic proteinReferences: 1. Chiti, F.; Dobson, C. M.. In Annu. Rev. Biochem, Annual Reviews: Palo Alto, 2006; Vol. 75, pp 333-366.
2. Knowles, T. P.; Vendruscolo, M.; Dobson, C. M..Nat. Rev. Mol. Cell Biol. 2014, 15 (6), 384-396.
3. Hajduk, P. J.; Greer, J.. Nat. Rev. Drug Discovery 2007, 6 (3), 211-219.
4. YPY Lam; CA Wootton; I Hands-Portman, J Wei; CKC Chiu; I Romero-Canelon; F Lermyte; MP Barrow; PB O’Connor.
Chem. Comm. 2018, 54, 13853-13856
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