An enhancer peptide for membrane-disrupting antimicrobial peptides

BMC Microbiology

Research Article

Kohtaro Kusaka¹  Hong Zhang¹  Yusuke Kato¹  Yasushi Tamada¹  Masaomi Minaba¹  Satoshi Ueno² 

[1] Division of Insect Sciences, National Institute of Agrobiological Sciences, Oowashi 1-2, 305-8634, Tsukuba, Ibaraki, Japan;Division of Insect Sciences, National Institute of Agrobiological Sciences, Oowashi 1-2, 305-8634, Tsukuba, Ibaraki, Japan;Graduate School of Life and Environmental Sciences, University of Tsukuba, Tennoudai 1-1-1, 305-8572, Tsukuba, Ibaraki, Japan;

关键词: Cytoplasmic Membrane;    Calcein;    Enrofloxacin;    Membrane Disruption;    Acidic Amino Acid Residue;   

DOI  :  10.1186/1471-2180-10-46

 received in 2009-06-30, accepted in 2010-02-15,  发布年份 2010

来源: Springer

【 摘 要 】

BackgroundNP4P is a synthetic peptide derived from a natural, non-antimicrobial peptide fragment (pro-region of nematode cecropin P4) by substitution of all acidic amino acid residues with amides (i.e., Glu → Gln, and Asp → Asn).ResultsIn the presence of NP4P, some membrane-disrupting antimicrobial peptides (ASABF-α, polymyxin B, and nisin) killed microbes at lower concentration (e.g., 10 times lower minimum bactericidal concentration for ASABF-α against Staphylococcus aureus), whereas NP4P itself was not bactericidal and did not interfere with bacterial growth at ≤ 300 μg/mL. In contrast, the activities of antimicrobial agents with a distinct mode of action (indolicidin, ampicillin, kanamycin, and enrofloxacin) were unaffected. Although the membrane-disrupting activity of NP4P was slight or undetectable, ASABF-α permeabilized S. aureus membranes with enhanced efficacy in the presence of NP4P.ConclusionsNP4P selectively enhanced the bactericidal activities of membrane-disrupting antimicrobial peptides by increasing the efficacy of membrane disruption against the cytoplasmic membrane.

【 授权许可】

Unknown   
© Ueno et al; licensee BioMed Central Ltd. 2010. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.