Design and activity study of a melittin-thanatin hybrid peptide

被引:16
作者
Jiang, Xiaofeng [1 ,4 ,5 ]
Qian, Kun [2 ]
Liu, Guangping [1 ,3 ]
Sun, Laiyu [2 ]
Zhou, Guoqing [2 ]
Li, Jingfen [2 ]
Fang, Xinqiang [2 ]
Ge, Haixia [2 ]
Lv, Zhengbing [1 ,5 ]
机构
[1] Zhejiang Sci Tech Univ, Coll Life Sci & Med, Hangzhou 310018, Zhejiang, Peoples R China
[2] Huzhou Univ, Sch Life Sci, Huzhou 313000, Zhejiang, Peoples R China
[3] Yanan Univ, Coll Life Sci, Yanan 716000, Shaanxi, Peoples R China
[4] Zhejiang Univ, Sch Life Sci, Hangzhou 31058, Zhejiang, Peoples R China
[5] Hangzhou Huadihlth Grp Ltd Co, Hangzhou 31012, Zhejiang, Peoples R China
关键词
Melittin; Thanatin; Hybrid peptide; Structure; Activity; INDUCED CYTOGENETIC DAMAGE; GRAM-NEGATIVE BACTERIA; ANTIMICROBIAL PEPTIDE; IN-VITRO; ANTIBACTERIAL; ANALOGS; EXPRESSION; FUSION; CYTOTOXICITY; PROTEGRIN-1;
D O I
10.1186/s13568-019-0739-z
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
The unique antimicrobial mechanism of antimicrobials make them a promising substitute for antibiotics for fighting drug-resistant bacteria. Both melittin and thanatin have antimicrobial bioactivity. However, thanatin does not inhibit the growth of Staphylococcus aureus. Melittin can inhibit S. aureus and has strong hemolytic activity. In the present study, the mutant fragments of melittin and thanatin were combined by flexible peptides to form a novel hybrid peptide, which was synthesized based on the secondary and tertiary structure prediction. The hybrid peptide inhibited S. aureus with a hemolytic concentration of above 45mol/L and inhibition rate in SMMC-7721 cells of 19.14%. The hybrid antimicrobial peptide, which was designed by the combination of -helix and -lamellar antimicrobial peptides, showed that both types of peptides did not interact with each either on spatial structure or biological activities, thereby providing a novel idea for the design of artificial antimicrobial peptides.
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页数:6
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