Acta Veterinaria et Zootechnica Sinica ›› 2022, Vol. 53 ›› Issue (6): 1905-1913.doi: 10.11843/j.isn.0366-6964.2022.06.024

• BASIC VETERINARY MEDICINE • Previous Articles     Next Articles

Molecular Design, Structure and Activity Analysis of Antimicrobial Peptide Tachyplesin I

SUN Dong1, CAI Yinchuan2, JIANG Siyu1, LI Xuan3, HAO Gang1*   

  1. 1. College of Food Science and Technology, Southwest Minzu University, Chengdu 610041, China;
    2. The Research Institute of Industrial Economy of Aba, Wenchuan 623000, China;
    3. Chongqing Academy of Metrology and Quality Inspection, Chongqing 401120, China
  • Received:2021-06-20 Online:2022-06-23 Published:2022-06-25

Abstract: Based on the structure-activity relationship of the antimicrobial peptide tachyplesin Ⅰ(TP Ⅰ), a novel antimicrobial peptide TP Ⅰ-Y4 was designed out. TP Ⅰ-Y4 was obtained by replacing four cysteines with tyrosines to delete two disulfide bonds of TP Ⅰ, keeping the chain length and charge number of the parent peptide. The results of bioinformatics software analysis had discovered that compared with TP Ⅰ, TP Ⅰ-Y4 had better thermal stability, stronger hydrophilicity, and similar structure and antibacterial activity to propeptide. After chemical synthesis, the results of circular dichroism spectroscopy had showed that TP Ⅰ-Y4 also adopted β-sheet structure in aqueous phase and 50% trifluoroethanol solution which simulated the hydrophobic environment of cell membrane. The β-sheet contents of TP Ⅰ-Y4 in hydrophobic environment were higher than that in aqueous phase. TP Ⅰ-Y4 exhibited higher β-sheet contents than TP Ⅰ in different environments. TP Ⅰ-Y4 owned potent antimicrobial activities against bacteria and fungi, and TP Ⅰ-Y4 displayed stronger antimicrobial activities against bacteria tested than TP Ⅰ. TP Ⅰ-Y4 reduced the hemolysis of mouse red blood cells and retained a strong endotoxin neutralization ability, the neutralization rate reached more than 50% when the concentration was 40 μg·mL-1. The results suggest that the increase of TP I-Y4 antibacterial activity and the decrease of hemolytic activity may be related to the substitution of tyrosine, as β-sheet strong-former which further leads to the enhancement of β-sheet structure in antimicrobial peptide.

Key words: antimicrobial peptide, Tachyplesin Ⅰ, molecular design, circular dichroism, antimicrobial activity

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