The removal of disulfide bonds in amylin oligomers leads to the conformational change of the 'native' amylin oligomers.
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.
Department of Chemistry, Ben-Gurion University of the Negev, P.O. Box 653, Beér Sheva 84105, Israel. ymiller@bgu.ac.il.
Vered
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Wineman-Fisher
Lucia
L
Tudorachi
Einav
E
Nissim
Yifat
Y
Miller
D004220:Disulfides / Q000737:chemistry*; D058228:Islet Amyloid Polypeptide / Q000737:chemistry*; D056004:Molecular Dynamics Simulation; D055503:Protein Multimerization; D017433:Protein Structure, Secondary
D004220:Disulfides; D058228:Islet Amyloid Polypeptide