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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

Online
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1437-4315
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Volume 393, Issue 7

Issues

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

Lan Wang
  • Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084, China
  • These authors contributed equally to this work.
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Qian Liu
  • Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084, China
  • These authors contributed equally to this work.
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Jin-Chun Chen / Yi-Xian Cui / Bing Zhou / Yong-Xiang Chen
  • Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084, China
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Yu-Fen Zhao
  • Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084, China
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Yan-Mei Li
  • Corresponding author
  • Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084, China
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  • Other articles by this author:
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Abstract

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.

Keywords: antimicrobial; aggregation; hIAPP; membrane disruption

About the article

Corresponding author


Received: 2012-01-21

Accepted: 2012-04-16

Published in Print: 2012-07-01


Citation Information: , Volume 393, Issue 7, Pages 641–646, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/hsz-2012-0107.

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©2012 by Walter de Gruyter Berlin Boston.Get Permission

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