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从非洲爪蟾皮肤中分离出的新型短抗菌肽。

Novel short antimicrobial peptide isolated from Xenopus laevis skin.

作者信息

Zhang Yu, Liu Songcai, Li Siming, Cheng Yunyun, Nie Linyan, Wang Gang, Lv Chen, Wei Wenzhen, Cheng Cheng, Hou Feng, Hao Linlin

机构信息

College of Animal Science, Jilin University, Changchun, Jilin Province, 130062, China.

Five-Star Animal Health Pharmaceutical Factory of Jilin Province, Changchun, Jilin Province, 130062, China.

出版信息

J Pept Sci. 2017 May;23(5):403-409. doi: 10.1002/psc.2990. Epub 2017 Mar 16.

DOI:10.1002/psc.2990
PMID:28299865
Abstract

A rich source of bioactive peptides, including a large number of antimicrobial peptides, has been found in amphibian skin. In this study, a novel short antimicrobial peptide was purified from Xenopus laevis skin and characterised through reversed-phase high-performance liquid chromatography, Edman degradation and matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry. The peptide was composed of six amino acids with a sequence of DEDLDE and thus named X. laevis antibacterial peptide-P2 (XLAsp-P2). Transmission electron microscopy revealed that this peptide showed potential antimicrobial abilities against bacteria by damaging the bacterial cell membrane. XLAsp-P2 maybe inhibit bacterial growth by binding to the microbial genomic DNA. The peptide also exhibited a weak haemolytic activity against rabbit red blood cells. Therefore, XLAsp-P2 is a novel short anionic antibacterial peptide with broad activities. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd.

摘要

在两栖动物皮肤中发现了丰富的生物活性肽来源,其中包括大量抗菌肽。在本研究中,从非洲爪蟾皮肤中纯化出一种新型短抗菌肽,并通过反相高效液相色谱、埃德曼降解法和基质辅助激光解吸/电离飞行时间质谱对其进行了表征。该肽由六个氨基酸组成,序列为DEDLDE,因此命名为非洲爪蟾抗菌肽-P2(XLAsp-P2)。透射电子显微镜显示,该肽通过破坏细菌细胞膜对细菌表现出潜在的抗菌能力。XLAsp-P2可能通过与微生物基因组DNA结合来抑制细菌生长。该肽对兔红细胞也表现出较弱的溶血活性。因此,XLAsp-P2是一种具有广泛活性的新型短阴离子抗菌肽。版权所有©2017欧洲肽学会和约翰·威利父子有限公司。

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