Does deamidation of islet amyloid polypeptide accelerate amyloid fibril formation?

Research output: Contribution to journalArticle

Authors

  • Yuko P. Y. Lam
  • Christopher A. Wootton
  • Ian J. Hands-portman
  • Juan Wei
  • Cookson K. C. Chiu
  • Frederik Lermyte
  • Mark P. Barrow
  • Peter B. O'connor

Colleges, School and Institutes

Abstract

Mass spectrometry has been applied to determine the deamidation sites and the aggregation region of the deamidated human islet amyloid polypeptide (hIAPP). Mutant hIAPP with iso-aspartic residue mutations at possible deamidation sites showed very different fibril formation behaviour, which correlates with the observed deamidation-induced acceleration of hIAPP aggregation.

Details

Original languageEnglish
Pages (from-to)13853-13856
Number of pages4
JournalChemical Communications
Volume54
Issue number98
Publication statusPublished - 19 Nov 2018