Does deamidation of islet amyloid polypeptide accelerate amyloid fibril formation?†
Yuko P. Y.
Lam, 
a
Christopher A.
Wootton,
a
Ian
Hands-Portman,
b
Juan
Wei,
a
Cookson K. C.
Chiu,
a
Isolda
Romero-Canelon,
ac
Frederik
Lermyte,
a
Mark P.
Barrow
a
and
Peter B.
O’Connor
*a
a
Christopher A.
Wootton,
a
Ian
Hands-Portman,
b
Juan
Wei,
a
Cookson K. C.
Chiu,
a
Isolda
Romero-Canelon,
ac
Frederik
Lermyte,
a
Mark P.
Barrow
a
and
Peter B.
O’Connor
*a
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.
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