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牙鲆脂多糖结合蛋白/杀菌通透性增加蛋白（LBP/BPI）衍生肽的抗菌活性

Antimicrobial activity of peptides derived from olive flounder lipopolysaccharide binding protein/bactericidal permeability-increasing protein (LBP/BPI).

作者信息

Nam Bo-Hye, Moon Ji-Young, Park Eun-Hee, Kim Young-Ok, Kim Dong-Gyun, Kong Hee Jeong, Kim Woo-Jin, Jee Young Ju, An Cheul Min, Park Nam Gyu, Seo Jung-Kil

机构信息

Biotechnology Research Division, National Fisheries Research and Development Institute, Haean-ro 216, Gijang-eup, Gijang-gun, Busan 619-705, Korea.

Department of Biotechnology, Pukyong National University, Busan 608-737, Korea.

出版信息

Mar Drugs. 2014 Oct 17;12(10):5240-57. doi: 10.3390/md12105240.

DOI:10.3390/md12105240
PMID:25329706
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4210897/
Abstract

We describe the antimicrobial function of peptides derived from the C-terminus of the olive flounder LBP BPI precursor protein. The investigated peptides, namely, ofLBP1N, ofLBP2A, ofLBP4N, ofLBP5A, and ofLBP6A, formed α-helical structures, showing significant antimicrobial activity against several Gram-negative bacteria, Gram-positive bacteria, and the yeast Candida albicans, but very limited hemolytic activities. The biological activities of these five analogs were evaluated against biomembranes or artificial membranes for the development of candidate therapeutic agents. Gel retardation studies revealed that peptides bound to DNA and inhibited migration on an agarose gel. In addition, we demonstrated that ofLBP6A inhibited polymerase chain reaction. These results suggested that the ofLBP-derived peptide bactericidal mechanism may be related to the interaction with intracellular components such as DNA or polymerase.

摘要

我们描述了源自牙鲆LBP BPI前体蛋白C末端的肽的抗菌功能。所研究的肽，即ofLBP1N、ofLBP2A、ofLBP4N、ofLBP5A和ofLBP6A，形成了α-螺旋结构，对几种革兰氏阴性菌、革兰氏阳性菌和白色念珠菌表现出显著的抗菌活性，但溶血活性非常有限。针对生物膜或人工膜评估了这五种类似物的生物活性，以开发候选治疗剂。凝胶阻滞研究表明，肽与DNA结合并抑制其在琼脂糖凝胶上的迁移。此外，我们证明ofLBP6A抑制聚合酶链反应。这些结果表明，ofLBP衍生肽的杀菌机制可能与与DNA或聚合酶等细胞内成分的相互作用有关。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9c20/4210897/8c597433c5cc/marinedrugs-12-05240-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9c20/4210897/90d8daaa8db2/marinedrugs-12-05240-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9c20/4210897/152051336763/marinedrugs-12-05240-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9c20/4210897/061f7c6fcd67/marinedrugs-12-05240-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9c20/4210897/02dd3cb02b75/marinedrugs-12-05240-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9c20/4210897/39899f5ba85f/marinedrugs-12-05240-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9c20/4210897/7039ea106aab/marinedrugs-12-05240-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9c20/4210897/ca1af4f054e3/marinedrugs-12-05240-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9c20/4210897/8c597433c5cc/marinedrugs-12-05240-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9c20/4210897/90d8daaa8db2/marinedrugs-12-05240-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9c20/4210897/152051336763/marinedrugs-12-05240-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9c20/4210897/061f7c6fcd67/marinedrugs-12-05240-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9c20/4210897/02dd3cb02b75/marinedrugs-12-05240-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9c20/4210897/39899f5ba85f/marinedrugs-12-05240-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9c20/4210897/7039ea106aab/marinedrugs-12-05240-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9c20/4210897/ca1af4f054e3/marinedrugs-12-05240-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9c20/4210897/8c597433c5cc/marinedrugs-12-05240-g008.jpg

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