期刊
BIOPOLYMERS
卷 102, 期 1, 页码 58-68出版社
WILEY
DOI: 10.1002/bip.22399
关键词
cationic antimicrobial peptide; alanine substitution; Porphyromonas gingivalis; giant unilamellar vesicle; membrane-active peptide
资金
- KAKENHI, Ministry of Education, Culture, Sports, Science and Technology of Japan [2060725, 23560939]
- Development of Fundamental Technology for Analysis and Evaluation of Functional Agricultural Products and Functional Foods
- Grants-in-Aid for Scientific Research [23560939] Funding Source: KAKEN
The antimicrobial activity of analogs obtained by substituting arginine and lysine in CL(14-25), a cationic alpha-helical dodecapeptide, with alanine against Porphyromonas gingivalis, a periodontal pathogen, varied significantly depending on the number and position of cationic amino acids. The alanine-substituted analogs had no hemolytic activity, even at a concentration of 1 mM. The antimicrobial activities of CL(K20A) and CL(K20A, K25A) were 3.8-fold and 9.1-fold higher, respectively, than that of CL(14-25). The antimicrobial activity of CL(R15A) was slightly lower than that of CL(14-25), suggesting that arginine at position 15 is not essential but is important for the antimicrobial activity. The experiments in which the alanine-substituted analogs bearing the replacement of arginine at position 24 and/or lysine at position 25 were used showed that arginine at position 24 was crucial for the antimicrobial activity whenever lysine at position 25 was substituted with alanine. Helical wheel projections of the alanine-substituted analogs indicate that the hydrophobicity in the vicinity of leucine at position 16 and alanines at positions 18 and/or 21 increased by substituting lysine at positions 20 and 25 with alanine, respectively. The degrees of diSC(3)-5 release from P. gingivalis cells and disruption of GUVs induced by the alanine-substituted analogs with different positive charges were not closely related to their antimicrobial activities. The enhanced antimicrobial activities of the alanine-substituted analogs appear to be mainly attributable to the changes in properties such as hydrophobicity and amphipathic propensity due to alanine substitution and not to their extents of positive charge (cationicity). (C) 2013 Wiley Periodicals, Inc.
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