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

Xinwei Ge, Aleksandr Kakinen, Esteban N. Gurzov, Wen Yang, Lokman Pang, Emily H. Pilkington, Praveen Nedumpully-Govindan, Pengyu Chen, Frances Separovic, Thomas P. Davis, Pu Chun Ke, Feng Ding

Research output: Contribution to journalArticleResearchpeer-review

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.

Original languageEnglish
Pages (from-to)9394-9397
Number of pages4
JournalChemical Communications
Volume53
Issue number68
DOIs
Publication statusPublished - 2017

Cite this

Ge, Xinwei ; Kakinen, Aleksandr ; Gurzov, Esteban N. ; Yang, Wen ; Pang, Lokman ; Pilkington, Emily H. ; Nedumpully-Govindan, Praveen ; Chen, Pengyu ; Separovic, Frances ; Davis, Thomas P. ; Ke, Pu Chun ; Ding, Feng. / Zinc-coordination and C-peptide complexation : A potential mechanism for the endogenous inhibition of IAPP aggregation. In: Chemical Communications. 2017 ; Vol. 53, No. 68. pp. 9394-9397.
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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.",
author = "Xinwei Ge and Aleksandr Kakinen and Gurzov, {Esteban N.} and Wen Yang and Lokman Pang and Pilkington, {Emily H.} and Praveen Nedumpully-Govindan and Pengyu Chen and Frances Separovic and Davis, {Thomas P.} and Ke, {Pu Chun} and Feng Ding",
year = "2017",
doi = "10.1039/c7cc04291d",
language = "English",
volume = "53",
pages = "9394--9397",
journal = "Chemical Communications",
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Ge, X, Kakinen, A, Gurzov, EN, Yang, W, Pang, L, Pilkington, EH, Nedumpully-Govindan, P, Chen, P, Separovic, F, Davis, TP, Ke, PC & Ding, F 2017, 'Zinc-coordination and C-peptide complexation: A potential mechanism for the endogenous inhibition of IAPP aggregation' Chemical Communications, vol. 53, no. 68, pp. 9394-9397. https://doi.org/10.1039/c7cc04291d

Zinc-coordination and C-peptide complexation : A potential mechanism for the endogenous inhibition of IAPP aggregation. / Ge, Xinwei; Kakinen, Aleksandr; Gurzov, Esteban N.; Yang, Wen; Pang, Lokman; Pilkington, Emily H.; Nedumpully-Govindan, Praveen; Chen, Pengyu; Separovic, Frances; Davis, Thomas P.; Ke, Pu Chun; Ding, Feng.

In: Chemical Communications, Vol. 53, No. 68, 2017, p. 9394-9397.

Research output: Contribution to journalArticleResearchpeer-review

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T1 - Zinc-coordination and C-peptide complexation

T2 - A potential mechanism for the endogenous inhibition of IAPP aggregation

AU - Ge, Xinwei

AU - Kakinen, Aleksandr

AU - Gurzov, Esteban N.

AU - Yang, Wen

AU - Pang, Lokman

AU - Pilkington, Emily H.

AU - Nedumpully-Govindan, Praveen

AU - Chen, Pengyu

AU - Separovic, Frances

AU - Davis, Thomas P.

AU - Ke, Pu Chun

AU - Ding, Feng

PY - 2017

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AB - 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.

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U2 - 10.1039/c7cc04291d

DO - 10.1039/c7cc04291d

M3 - Article

VL - 53

SP - 9394

EP - 9397

JO - Chemical Communications

JF - Chemical Communications

SN - 1359-7345

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