Structure-activity analysis of an antimicrobial peptide derived from bovine apolipoprotein A-II.

Structure-activity analysis of an antimicrobial peptide derived from bovine apolipoprotein A-II. Research Abstract Details 

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Structure-activity analysis of an antimicrobial peptide derived from bovine apolipoprotein A-II. Abstract Text:

Mitsuyoshi Motizuki,Takanori Satoh,Toshiaki Takei,Takehito Itoh,Sadaki Yokota,Shuichi Kojima,Kin-ichiro Miura,Tatsuya Samejima,Kunio Tsurugi,

We previously showed that bovine apolipoprotein A-II (apoA-II) has antimicrobial activity against Escherichia coli in PBS, and its C-terminal residues 49-76 are responsible for the activity using synthetic peptides. In order to understand the structural requirements of peptide 49-76 for the antimicrobial activity, the N- or C-terminus was truncated and then the charged (Lys or Asp) or Ser residues were replaced by Ala. Deletion of the first or last three amino acids and replacement of Lys-54/55 or 71/72 by Ala caused a substantial decreases in alpha-helical content in 50% TFE, showing the possible presence of helices in N- and C-terminal regions, respectively. The anti-Escherichia coli activity of the peptide correlated with its liposome-binding activity. Replacement of Lys-54/55 or 71/72 by Ala resulted in an almost complete loss of anti-E. coli activity with a substantial decrease in liposome-binding activity. Moreover, deletion of the last three amino acids caused a reduction to 1/17 of the original anti-E. coli activity with a moderate decrease in liposome-binding activity. In contrast, replacement of Ser-65/66, Asp-59, or Asp-69 by Ala hardly affected the anti-E. coli activity. These findings suggest that Lys-54/55 and Lys-71/72 on the putative helices are critical for antimicrobial activity, and the C-terminal 3 amino acids are important for the structural integrity of the C-terminal region for effective antimicrobial activity.

Structure-activity analysis of an antimicrobial peptide derived from bovine apolipoprotein A-II. Publishing Authors By Initials

M Motizuki,T Satoh,T Takei,T Itoh,S Yokota,S Kojima,K Miura,T Samejima,K Tsurugi,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: structure-activity relationship research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: structure-activity relationship research

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Structure-activity analysis of an antimicrobial peptide derived from bovine apolipoprotein A-II. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 132

Page Numbers: 115-9

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jul

YEAR: 2002

Structure-activity analysis of an antimicrobial peptide derived from bovine apolipoprotein A-II. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Structure-activity analysis of an antimicrobial peptide derived from bovine apolipoprotein A-II. Keywords Mesh Terms:

KEYWORDS: Structure-Activity Relationship

MESH TERMS: metabolism

Chemical & Substance for Abstract: Structure-activity analysis of an antimicrobial peptide derived from bovine apolipoprotein A-II. Information

Substance Name: Peptides

Registry Number: 0

Grant and Affiliation Information for Structure-activity analysis of an antimicrobial peptide derived from bovine apolipoprotein A-II.

AFFILIATION: Department of Biochemistry Yamanashi Medical University, Nakakoma, Yamanashi 409-3898, Japan. mitsum@swallow.res.yamanashi-med.ac.jp

Country: Japan

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MEDLINETA: J Biochem

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