Does deamidation of islet amyloid polypeptide accelerate amyloid fibril formation?

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

Research output: Contribution to journalArticlepeer-review

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

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