Zinc stabilization of prefibrillar oligomers of human islet amyloid polypeptide

被引：68

作者：

Brender, Jeffrey R. ^{[1
,2
]}

Krishnamoorthy, Janarthanan ^{[1
,2
]}

Messina, Grazia M. L. ^{[3
]}

Deb, Aniruddha ^{[1
,2
]}

Vivekanandan, Subramanian ^{[1
,2
]}

La Rosa, Carmelo ^{[3
]}

Penner-Hahn, James E. ^{[1
,2
]}

Ramamoorthy, Ayyalusamy ^{[1
,2
]}

机构：

[1] Univ Michigan, Ann Arbor, MI 48109 USA

[2] Univ Michigan, Dept Chem, Ann Arbor, MI 48109 USA

[3] Univ Catania, Dept Chem Sci, I-95125 Catania, Italy

来源：

CHEMICAL COMMUNICATIONS | 2013年 / 49卷 / 32期

关键词：

MEMBRANE DISRUPTION; EARLY EVENTS; NMR; IAPP; MECHANISM; PEPTIDE; BINDING; ASSOCIATION; INHIBITION;

D O I：

10.1039/c3cc40383a

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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.

引用

页码：3339 / 3341

页数：3

共 24 条

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