Collagencin, an antibacterial peptide from fish collagen: Activity, structure and interaction dynamics with membrane
Collagencin, an antibacterial peptide from fish collagen: Activity, structure and interaction dynamics with membrane
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DOI：
10.1016/j.bbrc.2016.03.121
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发表时间：
2016-04-29
影响因子：
3.1
通讯作者：
Fliss, Ismail
中科院分区：
文献类型：
--
作者：
Ennaas, Nadia;Hammami, Riadh;Fliss, Ismail
在这项研究中，我们首先报告的胶原蛋白，抗菌肽从鱼胶原蛋白水解物鉴定的表征。肽完全抑制金黄色葡萄球菌在1.88 mM的生长。虽然无毒高达470 μ M，胶原蛋白是溶血性在较高浓度。CD和分子动力学分析表明胶原蛋白的二级结构主要由β折叠和β转角组成。该肽可能在疏水环境下形成β-折叠结构，并与阴离子（磷脂酰甘油）和两性离子（磷酸乙醇胺和磷脂酰胆碱）脂质相互作用，如CD光谱和分子动力学所示。该肽与POPG和POPE脂质形成多个氢键，并保留在膜-水界面上，表明胶原蛋白抗菌作用遵循地毯式机制。胶原蛋白鱼废料可以通过酶水解处理并转化为具有功能或生物特性的高价值产品。海洋胶原蛋白是一种很有前途的抗菌肽来源，在食品安全和人类健康方面具有新的意义。(C)2016 Elsevier Inc. All rights reserved.
In this study, we first report characterization of collagencin, an antimicrobial peptide identified from fish collagen hydrolysate. The peptide completely inhibited the growth of Staphylococcus aureus at 1.88 mM. Although non-toxic up to 470 mu M, collagencin was hemolytic at higher concentrations. The secondary structure of collagencin was mainly composed by beta-sheet and beta-turn as determined by CD measurements and molecular dynamics. The peptide is likely to form beta-sheet structure under hydrophobic environments and interacts with both anionic (phosphatidylglycerol) and zwitterionic (phosphoethanolamine and phosphatidylcholine) lipids as shown with CD spectroscopy and molecular dynamics. The peptide formed several hydrogen bonds with both POPG and POPE lipids and remained at membrane water interface, suggesting that collagencin antibacterial action follows a carpet mechanism. Collagenous fish wastes could be processed by enzymatic hydrolysis and transformed into products of high value having functional or biological properties. Marine collagens are a promising source of antimicrobial peptides with new implications in food safety and human health. (C) 2016 Elsevier Inc. All rights reserved.