韩国本土山羊乳铁蛋白的抗菌肽及其活性关键部位的鉴定

Antimicrobial peptide of korean native goat lactoferrin and identification of the part essential for this activity.

作者信息

Kimura M, Nam M S, Ohkouchi Y, Kumura H, Shimazaki K i, Yu D Y

机构信息

Dairy Science Laboratory, Department of Animal Product Science, Graduate School of Agriculture, Hokkaido University, Sapporo, 060-8589, Japan.

出版信息

Biochem Biophys Res Commun. 2000 Feb 16;268(2):333-6. doi: 10.1006/bbrc.2000.2141.

DOI:10.1006/bbrc.2000.2141

PMID:10679204

Abstract

The antimicrobial activity of lactoferrin isolated from Korean native goat (KN goat) milk was studied and its antimicrobial domain was identified using synthetic peptides. Antimicrobial activity was assayed by a micro-method using 96-well microplates and a microplate reader. The amino acid sequence of the antimicrobial domain was suggested to be YQWQRRMRKLGAPSIT and this sequence corresponds to amino acid residues 20 to 35 of KN goat lactoferrin. Five peptides with certain amino acid residues deleted were synthesized in an effort to identify the residues essential for antimicrobial activity and it was found that the part with the sequence RRMRK (24-28) is the region most important for this activity. On the other hand, the conformation of the peptides did not influence the antimicrobial activity.

摘要

研究了从韩国本土山羊（KN山羊）奶中分离出的乳铁蛋白的抗菌活性，并使用合成肽鉴定了其抗菌结构域。通过使用96孔微孔板和酶标仪的微量方法测定抗菌活性。抗菌结构域的氨基酸序列被认为是YQWQRRMRKLGAPSIT，该序列对应于KN山羊乳铁蛋白的第20至35个氨基酸残基。合成了五种缺失某些氨基酸残基的肽，以确定对抗菌活性至关重要的残基，结果发现序列RRMRK（24 - 28）所在部分对该活性最为重要。另一方面，肽的构象不影响抗菌活性。