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 |
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Pages (from-to) | 13853-13856 |
Number of pages | 4 |
Journal | Chemical Communications |
Volume | 54 |
Issue number | 98 |
DOIs | |
Publication status | Published - 19 Nov 2018 |