Antimicrobial activity and stability of the D-amino acid substituted derivatives of antimicrobial peptide polybia-MPI

doi:10.1186/s13568-016-0295-8

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	Antimicrobial activity and stability of the D-amino acid substituted derivatives of antimicrobial peptide polybia-MPI
	Zhao, YY; Zhang, M; Qiu, S; Wang, JY; Peng, JX; Zhao, P; Zhu, RR; Wang, HL; Li, Y; Wang, KR
刊名	AMB Express
	2016-11-29
卷号	6
关键词	Antimicrobial peptide Polybia-MPI Stability D-Amino acid substitution
ISSN号	2191-0855
DOI	10.1186/s13568-016-0295-8
文献子类	Article
英文摘要	Antimicrobial peptide has the potential to be developed as new kind of antimicrobial agents with novel action mechanism. However, the susceptibility to protease is a drawback for potential peptides to be clinical used. D-amino acid substitution can be one way to increase the proteolytic stability of peptides. In the present study, we synthesized the d-lysines substituted analog (d-lys-MPI) and the D-enantiomer of polybia-MPI (D-MPI) to improve the proteolytic resistance of polybia-MPI. Our results showed that, the stability of its D-amino acid partially substituted analog D-lys-MPI was increased. However, it lost antimicrobial activity at the tested concentration with the loss of a-helix content. As shown in the CD spectra, after substitution, the spectra of D-MPI is symmetrical to MPI, indicated it turned into left hand a-helical conformation. Excitingly, the stability of D-MPI toward the tested protease was improved greatly. Notably, the antimicrobial activity of D-MPI was comparable to its L-counterpart MPI, even improved. In addition, the hemolytic activity of D-MPI was lowered. This also indicated that the action target of antimicrobial peptide polybia-MPI was not chiral specific. So, D-MPI may offer a therapeutic strategy to defend the infection of microbes, considering its stability to protease and relatively lower cytotoxicity to human erythrocytes.
学科主题	Biotechnology & Applied Microbiology
出版地	LONDON
资助项目	国家自然科学基金项目 ; 中央高校基本科研业务费专项资金 ; 甘肃省自然科学基金计划
项目编号	National Natural Science Foundation of China [81573265, 91213302, 21272108, 81473095, 81260387, 81360112] ; Natural Science Foundation of Gansu Province, China [1208RJZ109, 1606RJA159] ; Fundamental Research Funds for the Central Universities [lzujbky-2015-279, lzujbky-2015-k11, lzujbky-2016-ct01]
语种	英语
WOS记录号	WOS:000389486200001
资助机构	NSFC ; LZU ; GSSTD
内容类型	期刊论文
源URL	[http://ir.lzu.edu.cn/handle/262010/188724]
专题	基础医学院_期刊论文
通讯作者	Wang, KR; Yan, WJ; Wang, R (reprint author), Lanzhou Univ, Sch Basic Med Sci, Key Lab Preclin Study New Drugs Gansu Prov, 222 Tian Shui South Rd, Lanzhou 730000, Peoples R China.
推荐引用方式 GB/T 7714	Zhao, YY,Zhang, M,Qiu, S,et al. Antimicrobial activity and stability of the D-amino acid substituted derivatives of antimicrobial peptide polybia-MPI[J]. AMB Express,2016,6.
APA	Zhao, YY.,Zhang, M.,Qiu, S.,Wang, JY.,Peng, JX.,...&Wang, R .(2016).Antimicrobial activity and stability of the D-amino acid substituted derivatives of antimicrobial peptide polybia-MPI.AMB Express,6.
MLA	Zhao, YY,et al."Antimicrobial activity and stability of the D-amino acid substituted derivatives of antimicrobial peptide polybia-MPI".AMB Express 6(2016).