Previously, we purified a serine protease with a molecular mass of 26 kDa that exhibits potent antibacterial activity from a pupal extract of Sarcophaga peregrina (flesh fly). We divided this protease into 12 peptides and examined their antibacterial activity. A peptide corresponding to residues 155 to 174 (peptide 9) was found to exhibit antibacterial activity comparable to that of the 26-kDa protease. When Escherichia coli was treated with peptide 9, the permeability of both the outer and inner membranes increased, and substrates for beta-lactamase and beta-galactosidase entered the cells, but beta-galactosidase did not leak out of the cells under these conditions. It was suggested that residues 6 to 18 of peptide 9 form an amphiphilic alpha-helix under hydrophobic conditions with an N-terminal basic loop and then interact with acidic phospholipids in the bacterial membranes.

译文

以前,我们从sarcopoga peregrina (肉蝇) 的p提取物中纯化了分子量为26 kDa的丝氨酸蛋白酶,该蛋白酶具有有效的抗菌活性。我们将这种蛋白酶分为12个肽,并检查了它们的抗菌活性。发现对应于残基155至174的肽 (肽9) 表现出与26-kda蛋白酶相当的抗菌活性。当用肽9处理大肠杆菌时,外膜和内膜的通透性均增加,β-内酰胺酶和 β-半乳糖苷酶的底物进入细胞,但在这些条件下 β-半乳糖苷酶不会泄漏出细胞。建议肽9的残基6至18在疏水条件下形成具有N末端碱性环的两亲性 α 螺旋,然后与细菌膜中的酸性磷脂相互作用。

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