肽
膜
抗菌肽
化学
脂质体
阳离子聚合
生物物理学
细菌
抗菌剂
细胞膜
脂质双层
生物化学
生物
有机化学
遗传学
作者
Isabel Pérez-Guillén,Òscar Domènech,Adrià Botet-Carreras,Alexandra Merlos,Josep M. Sierra,Fernando Alberício,Beatriz G. de la Torre,M. Teresa Montero,Miguel Viñas,Jordi Hernández-Borrell
出处
期刊:Pharmaceutics
[MDPI AG]
日期:2022-10-14
卷期号:14 (10): 2191-2191
被引量:2
标识
DOI:10.3390/pharmaceutics14102191
摘要
The super-cationic peptide dendrimers (SCPD) family is a valuable class of antimicrobial peptide candidates for the future development of antibacterial agents against multidrug-resistant gram-negative bacteria. The deep knowledge of their mechanism of action is a major challenge in research, since it may be the basis for future modifications/optimizations. In this work we have explored the interaction between SCPD and membranes through biophysical and microbiological approaches in the case of the G1OLO-L2OL2 peptide. Results support the idea that the peptide is not only adsorbed or close to the surface of the membrane but associated/absorbed to some extent to the hydrophobic-hydrophilic region of the phospholipids. The presence of low concentrations of the peptide at the surface level is concomitant with destabilization of the cell integrity and this may contribute to osmotic stress, although other mechanisms of action cannot be ruled out.
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