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

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Zinc-coordination and C-peptide complexation: a potential mechanism for the endogenous inhibition of IAPP aggregation
Chemical Communications ( IF 4.9 ) Pub Date : 2017-07-19 00:00:00 , DOI: 10.1039/c7cc04291d
Xinwei Ge _{1,

2,

3,

4} , Aleksandr Kakinen _{5,

6,

7,

8,

9} , Esteban N. Gurzov _{9,

10,

11,

12,

13} , Wen Yang _{4,

14,

15} , Lokman Pang _{9,

10,

11,

12,

13} , Emily H. Pilkington _{5,

6,

7,

8,

9} , Praveen Govindan-Nedumpully _{1,

2,

3,

4} , Pengyu Chen _{4,

14,

15} , Frances Separovic _{9,

16,

17,

18,

19} , Thomas P. Davis _{5,

6,

7,

8,

9} , Pu Chun Ke _{5,

6,

7,

8,

9} , Feng Ding _{1,

2,

3,

4}

Affiliation

Department of Physics and Astronomy
Clemson University
Clemson
USA
ARC Centre of Excellence in Convergent Bio-Nano Science and Technology
Monash Institute of Pharmaceutical Sciences
Monash University
Parkville
Australia
St Vincent's Institute of Medical Research
Fitzroy
Department of Medicine
St. Vincent's Hospital
Department of Material Engineering
Auburn
School of Chemistry
Bio21 Institute
University of Melbourne
Melbourne

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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