Antimicrobial activity of human islet amyloid polypeptides: an insight into amyloid peptides' connection with antimicrobial peptides

被引：39

作者：

Wang, Lan ^{[1
]}

Liu, Qian ^{[1
]}

Chen, Jin-Chun ^{[2
]}

Cui, Yi-Xian ^{[2
]}

Zhou, Bing ^{[2
]}

Chen, Yong-Xiang ^{[1
]}

Zhao, Yu-Fen ^{[1
]}

Li, Yan-Mei ^{[1
]}

机构：

[1] Tsinghua Univ, Key Lab Bioorgan Phosphorus Chem & Chem Biol, Minist Educ, Dept Chem, Beijing 100084, Peoples R China

[2] Tsinghua Univ, Sch Life Sci, Beijing 100084, Peoples R China

来源：

BIOLOGICAL CHEMISTRY | 2012年 / 393卷 / 07期

关键词：

antimicrobial; aggregation; hIAPP; membrane disruption; TYPE-2; DIABETES-MELLITUS; ALZHEIMERS-DISEASE; PROTEIN; CYTOTOXICITY; MEMBRANES; OLIGOMERS; AMYLIN;

D O I：

10.1515/hsz-2012-0107

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Human islet amyloid polypeptide (hIAPP) shows an antimicrobial activity towards two types of clinically relevant bacteria. The potency of hIAPP varies with its aggregation states. Circular dichroism was employed to determine the interaction between hIAPP and bacteria lipid membrane mimic. The antimicrobial activity of each aggregate species is associated with their ability to induce membrane disruption. Our findings provide new evidence revealing the antimicrobial activity of amyloid peptide, which suggest a possible connection between amyloid peptides and antimicrobial peptides.

引用

页码：641 / 646

页数：6

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