Issue 32, 2013
From the journal:

Chemical Communications

Zinc stabilization of prefibrillar oligomers of human islet amyloid polypeptide†

Jeffrey R. Brender,a   Janarthanan Krishnamoorthy,a   Grazia M. L. Messina,b   Aniruddha Deb,a   Subramanian Vivekanandan,a   Carmelo La Rosa,b   James E. Penner-Hahna  and  Ayyalusamy Ramamoorthy*a  

* Corresponding authors

a Biophysics and Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USA
E-mail: ramamoor@umich.edu
Tel: +1 734 647-6572

b Department of Chemical Sciences, University of Catania, Viale A. Doria 6, 95125 Catania, Italy

Abstract

The aggregation of human islet amyloid polypeptide (hIAPP) has been linked to beta-cell death in type II diabetes. Zinc present in secretory granules has been shown to affect this aggregation. A combination of EXAFS, NMR, and AFM experiments shows that the influence of zinc is most likely due to the stabilization of prefibrillar aggregates of hIAPP.

Graphical abstract: Zinc stabilization of prefibrillar oligomers of human islet amyloid polypeptide

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Article information

DOI
https://doi.org/10.1039/C3CC40383A
Article type
Communication
Submitted
16 ⵉⵏⵏ 2013
Accepted
06 ⵎⴰⵕ 2013
First published
06 ⵎⴰⵕ 2013

Chem. Commun., 2013,49, 3339-3341

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Zinc stabilization of prefibrillar oligomers of human islet amyloid polypeptide

J. R. Brender, J. Krishnamoorthy, G. M. L. Messina, A. Deb, S. Vivekanandan, C. La Rosa, J. E. Penner-Hahn and A. Ramamoorthy, Chem. Commun., 2013, 49, 3339 DOI: 10.1039/C3CC40383A

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