Abstract
The α-helical structure of the N-terminus of the 'native' amylin Lys1-Cys7 consists of a disulfide bond between Cys2 and Cys7. The 'native' amylin oligomers demonstrate polymorphic states. Removal of the disulfide bonds in the 'native' amylin oligomers decreases the polymorphism and induces the formation of longer stable cross-β strands in the N-termini.
Highlights
The a-helical structure of the N-terminus of the ‘native’ amylin Lys1–Cys[7] consists of a disulfide bond between Cys[2] and Cys[7]
The common hallmarks of these amyloidogenic diseases are the deposition of misfolded proteins, such as Ab deposits in Alzheimer’s disease (AD), a-synuclein in Parkinson’s disease (PD) and amylin or human Islet amyloid polypeptide in Type 2 diabetes (T2D)
We focus on how the removal of the disulfide bonds affects the morphology of amylin oligomers, the conformational change of the various amylin oligomers and the populations
Summary
The a-helical structure of the N-terminus of the ‘native’ amylin Lys1–Cys[7] consists of a disulfide bond between Cys[2] and Cys[7]. Removal of the disulfide bonds in the ‘native’ amylin oligomers decreases the polymorphism and induces the formation of longer stable cross-b strands in the N-termini. In models E1–E4 the disulfide bonds were removed and the N-termini (Lys1–Cys7) of the amylin monomers were extended to form b-strand structures.
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