Poster Presentation 12th Australian Peptide Conference 2017

Non-covalent sulfur-oxygen interactions control conformation in a peptidomimetic that disrupts islet amyloid polypeptide fibrillation  (#181)

Hayden J Peacock 1 , Tohru Yamashita 2 , Jinghui Luo 2 , James Luccarelli 2 , Sam Thompson 3 , Andrew D Hamilton 4
  1. Institute for Molecular Bioscience, University of Queensland, St Lucia, QLD, Australia
  2. Department of Chemistry, University of Oxford, Oxford, UK
  3. Department of Chemistry, University of Southampton, Southampton, UK
  4. Department of Chemistry, New York University, New York, USA

Here we report the use of sulfur-oxygen interactions as a conformational control element in a new class of peptidomimetic scaffolds. Solution and solid-state conformational analysis indicates that the scaffolds mimic key elements of alpha-helical secondary structure. The molecules disrupt the fibrillation of islet amyloid polypeptide (IAPP), a process that is implicated in the pathology of type II diabetes, most likely operating via an alpha-helix-dependent mechanism.