Design and characterization of novel hybrid peptides from LFB15(W4,10), HP(2-20), and cecropin A based on structure parameters by computer-aided method |
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Authors: | Zi-gang Tian Tian-tang Dong Da Teng Ya-lin Yang Jian-hua Wang |
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Institution: | (1) Gene Engineering Laboratory, Feed Research Institute, Chinese Academy of Agricultural Sciences, 12 Zhongguancun Nandajie St., Haidian District, Beijing, 100081, People’s Republic of China |
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Abstract: | The increasing problem of antibiotic resistance among pathogenic bacteria requires development of new antimicrobial agents.
The pivotal assets of the antimicrobial peptide include potential for rapid bactericidal activity and low propensity for resistance.
The four new antimicrobial hybrid peptides were designed based on peptides LFB15(W4,10), HP(2-20), and cecropin A according
to the structure–activity relationship of the amphipathic and cationic antimicrobial peptides. Their structural parameters
were accessed by bioinformatics tools, and then two hybrids with the most potential candidates were synthesized. The hybrid
peptide LH28 caused an increase in antibiotic activity (MIC50 = 1.56–3.13 μM) against given bacterial strains and did not cause obvious hemolysis of rabbit erythrocytes at concentration
of 3.13 μM with effective antimicrobial activity. The results demonstrate that evaluating the structural parameters could
be useful for designing novel antimicrobial peptides.
Zi-gang Tian and Tian-tang Dong contributed equally to this paper |
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Keywords: | Antimicrobial peptides Design Structure parameters Computer-aided method |
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