抗菌肽Tachyplesin Ⅰ及衍生物对大肠杆菌细胞膜作用机制的对比研究

doi:10.11843/j.issn.0366-6964.2022.09.032

Abstract

Abstract: The action mechanism of antimicrobial peptide tachyplesin Ⅰ(TP Ⅰ) and its analogue TP Ⅰ-Y4 targeted the cell membrane of Escherichia coli have been studied by exploring the action mode of both peptides on the liposome membrane, the effect on the bacteria surface potential, hydrophobicity, the permeability of inner and outer membrane, and ion leakage after two peptides treated E.coli. The results showed that TP Ⅰ/TP Ⅰ-Y4 induced the increase of surface potential and hydrophobicity of E.coli. TP Ⅰ-Y4 caused a slightly higher potential and hydrophobicity enhancement than TP Ⅰ. Both peptides could disturb the liposome membrane causing the calcein leakage during peptides crossing phospholipids bilayer, TP Ⅰ-Y4 caused more fluorescein leakage, but it did not completely collapse the liposome membrane. TP Ⅰ/TP Ⅰ-Y4 obviously increased the inner and outer membrane permeability of bacteria, in contrast, TP Ⅰ-Y4 induced stronger outer membrane permeability, greater damage to the plasma membrane, causing more leakage of ions and intracellular macromolecules. TP Ⅰ-Y4 had a greater destructive effect on E.coli cell membrane, which may be the main reason for the significant improvement of its antibacterial activity compared with TP Ⅰ.

Key words: antimicrobial peptide, tachyplesin Ⅰ, analogue, Escherichia coli, membrane action mechanism

CLC Number:

S859.79
R978

SUN Dong, QU Sha, LI Xuan, TANG Shanhu, LI Sining, HAO Gang. Comparative Study on the Membrane Action Mechanism of Tachyplesin Ⅰ and Its Analogue on Escherichia coli[J]. Acta Veterinaria et Zootechnica Sinica, 2022, 53(9): 3180-3189.

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Comparative Study on the Membrane Action Mechanism of Tachyplesin Ⅰ and Its Analogue on Escherichia coli

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