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Cationic Antimicrobial Peptides (AMPs): Thermodynamic Characterization of Peptide–Lipid Interactions and Biological Efficacy of Surface‐Tethered Peptides

机译:阳离子抗菌肽(AMPs):肽-脂质相互作用的热力学表征和表面束缚肽的生物功效

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AbstractAntimicrobial peptides (AMPs) were investigated both as novel antibiotics and as antimicrobial coatings for biomedical implants. The hydrophobicity, conformational constraint, and strong binding of cyclo-RRRWFW (c-WFW) to the O-antigen region of lipopolysaccharide (LPS) were identified as important features for potent anti-E. coli activity. Furthermore, tethered membrane-active AMPs with uniform distribution of cationic and hydrophobic amino acid residue were identified as good anti-biofilm agents.
机译:摘要研究了抗菌肽(AMPs)作为新型抗生素和生物医学植入物的抗菌涂层。疏水性,构象约束,和环状RRRWFW(c-WFW)与脂多糖(LPS)的O抗原区域的牢固结合被确定为有效的抗E的重要特征。大肠杆菌活性。此外,具有均匀分布的阳离子和疏水氨基酸残基的束缚膜活性AMP被确定为良好的抗生物膜剂。

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    《ChemistryOpen》 |2015年第3期|共5页
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  • 中图分类 生物物理学;
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