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

doi:10.1039/C8CC06675B

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

Pharmacy

Research output: Contribution to journal › Article › peer-review

5 Citations (Scopus)

338 Downloads (Pure)

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 language	English
Pages (from-to)	13853-13856
Number of pages	4
Journal	Chemical Communications
Volume	54
Issue number	98
DOIs	https://doi.org/10.1039/C8CC06675B
Publication status	Published - 19 Nov 2018

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10.1039/C8CC06675BLicence: None: All rights reserved

Lam_et_al_Does_deamidation_of_islet_amyloid_Chemical_Communications_2018
Checked for eligibility 07/12/2018 This is a peer-reviewed version of an article published in Chemical Communications. Chem. Commun., 2018,54, 13853-13856 10.1039/C8CC06675B
Accepted author manuscript, 2.93 MBLicence: None: All rights reserved

https://pubs.rsc.org/en/content/articlelanding/2018/cc/c8cc06675bLicence: None: All rights reserved

Cite this

@article{0a679e702cf0476c868aa39c51cd4e81,

title = "Does deamidation of islet amyloid polypeptide accelerate amyloid fibril formation?",

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.",

author = "Lam, \{Yuko P. Y.\} and Wootton, \{Christopher A.\} and Hands-portman, \{Ian J.\} and Juan Wei and Chiu, \{Cookson K. C.\} and Isolda Romero-Canel{\'o}n and Frederik Lermyte and Barrow, \{Mark P.\} and O'connor, \{Peter B.\}",

year = "2018",

month = nov,

day = "19",

doi = "10.1039/C8CC06675B",

language = "English",

volume = "54",

pages = "13853--13856",

journal = "Chemical Communications ",

issn = "1359-7345",