Antibacterial activity of multiple antigen peptides homologous to a loop region in human lactoferrin

被引：26

作者：

Azuma, M

Kojima, T

Yokoyama, I

Tajiri, H

Yoshikawa, K

Saga, S

Del Carpio, CA

机构：

[1] Toyohashi Univ Technol, Dept Ecol Engn, Toyohashi, Aichi, Japan

[2] Nagoya Univ, Sch Med, Dept Surg 2, Nagoya, Aichi 466, Japan

[3] Natl Canc Hosp E, Dept Internal Med, Chiba, Japan

[4] Aichi Med Univ, Dept Pathol 2, Nagoya, Aichi, Japan

来源：

JOURNAL OF PEPTIDE RESEARCH | 1999年 / 54卷 / 03期

关键词：

antibacterial activity; lactoferrin; multiple antigen peptide; pore formation;

D O I：

10.1034/j.1399-3011.1999.00090.x

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

An 11-residue peptide (FQWQRNMRKVR) homologous to just over half the loop region of human lactoferricin is thought to be responsible for antimicrobial properties of human lactoferricin. Multiple antigen peptides (MAP) of the Ii-residue peptide exerted significant antibacterial effects against a broad spectrum of bacteria including MRSA. More than eight branching was favourable for increasing its antibacterial activity. Our report shows a novel possibility for MAP to increase the activity of antibiotic peptides other than simply to stimulate antibody production, as reported so far.

引用

页码：237 / 241

页数：5

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