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Zinc-coordination and C-peptide complexation: a potential mechanism for the endogenous inhibition of IAPP aggregation.


ABSTRACT: Aggregation of the highly amyloidogenic IAPP is endogenously inhibited inside beta-cell granules at millimolar concentrations. Combining in vitro experiments and computer simulations, we demonstrated that the stabilization of IAPP upon the formation of zinc-coordinated ion molecular complex with C-peptide might be important for the endogenous inhibition of IAPP aggregation.

SUBMITTER: Ge X 

PROVIDER: S-EPMC5570498 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature

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Zinc-coordination and C-peptide complexation: a potential mechanism for the endogenous inhibition of IAPP aggregation.

Ge Xinwei X   Kakinen Aleksandr A   Gurzov Esteban N EN   Yang Wen W   Pang Lokman L   Pilkington Emily H EH   Govindan-Nedumpully Praveen P   Chen Pengyu P   Separovic Frances F   Davis Thomas P TP   Ke Pu Chun PC   Ding Feng F  

Chemical communications (Cambridge, England) 20170801 68


Aggregation of the highly amyloidogenic IAPP is endogenously inhibited inside beta-cell granules at millimolar concentrations. Combining in vitro experiments and computer simulations, we demonstrated that the stabilization of IAPP upon the formation of zinc-coordinated ion molecular complex with C-peptide might be important for the endogenous inhibition of IAPP aggregation. ...[more]

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