Design and activity study of a melittin–thanatin hybrid peptide

AMB Express

Xiaofeng Jiang¹  Guangping Liu¹  Zhengbing Lv¹  Guoqing Zhou²  Xinqiang Fang²  Haixia Ge²  Laiyu Sun²  Jingfen Li²  Kun Qian² 

[1] College of Life Sciences And Medicine, Zhejiang Sci-Tech University;School of Life Science, Huzhou University;

关键词: Melittin;    Thanatin;    Hybrid peptide;    Structure;    Activity;   

DOI  :  10.1186/s13568-019-0739-z

来源: DOAJ

【 摘 要 】

Abstract 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 45 μmol/L and inhibition rate in SMMC-7721 cells of 19.14%. The hybrid antimicrobial peptide, which was designed by the combination of α-helix and β-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.

【 授权许可】

Unknown