Characterization of a Novel Antimicrobial Peptide Isolated from Moringa oleifera Seed Protein Hydrolysates and Its Membrane Damaging Effects on Staphylococcus aureus.
Characterization of a Novel Antimicrobial Peptide Isolated from Moringa oleifera Seed Protein Hydrolysates and Its Membrane Damaging Effects on Staphylococcus aureus.
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DOI：
10.1021/acs.jafc.2c01335
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发表时间：
2022-05
影响因子：
6.1
通讯作者：
Qiong Zhao;Li He;Xuefeng Wang;Xuesong Ding;Lige Li;Yang Tian;Aixiang Huang
中科院分区：
文献类型：
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作者：
Qiong Zhao;Li He;Xuefeng Wang;Xuesong Ding;Lige Li;Yang Tian;Aixiang Huang
本研究试图从辣木籽蛋白水解物中鉴定和表征一种新型抗菌肽，命名为 MOp2，并阐明其对金黄色葡萄球菌的潜在抗菌作用。 MOp2的氨基酸序列为His-Val-Leu-Asp-Thr-Pro-Leu-Leu (HVLDTPLL)，被表征为β-折叠结构的疏水性阴离子AMP。 MOp2 在 2.0× MIC 时表现出可忽略不计的溶血活性，表明其对金黄色葡萄球菌的生长有抑制作用（MIC：2.204 mM）。在5%盐下仍保持90%以上的抗菌活性，在115℃高温30分钟时仍保持78%左右的抗菌活性。蛋白酶，特别是酸性蛋白酶，不同程度地降低了其抗菌活性。此外，MOp2通过增加膜通透性对金黄色葡萄球菌细胞造成不可逆的膜损伤，导致细胞内核苷酸池的释放。此外，分子对接表明，MOp2 可以通过氢键和疏水相互作用与二氢叶酸还原酶和 DNA 旋转酶相互作用，从而抑制金黄色葡萄球菌生长。总体而言，MOp2 可能是食品加工中针对金黄色葡萄球菌的潜在新型抗菌剂。
The present study sought to identify and characterize a novel antimicrobial peptide, named MOp2 from Moringa oleifera seed protein hydrolysates, and elucidate its potential antimicrobial effects on Staphylococcus aureus. MOp2, with the amino acid sequence of His-Val-Leu-Asp-Thr-Pro-Leu-Leu (HVLDTPLL), was characterized as a hydrophobic anionic AMP of the β-sheet structure. MOp2 exhibited negligible hemolytic activity at 2.0× MIC, suggesting its inhibitory effect on the growth of S. aureus (MIC: 2.204 mM). It maintained more than 90% of antimicrobial activity under 5% salt and about 78% of antimicrobial activity at a high temperature of 115 °C for 30 min. Protease, especially acid protease, reduced its antimicrobial activity to different extents. Moreover, MOp2 caused irreversible membrane damage to S. aureus cells by increasing the membrane permeability, resulting in the release of intracellular nucleotide pools. Additionally, molecular docking revealed that MOp2 could inhibit S. aureus growth by interacting with dihydrofolate reductase and DNA gyrase through hydrogen bonding and hydrophobic interactions. Overall, MOp2 could be a potential novel antimicrobial agent against S. aureus in food processing.