High pressure treatment promotes the deteriorating effect of cationic antimicrobial peptides on bacterial membranes

被引：0
|
作者：
Kriegler, Simon [1 ]
Jaworek, Michel W. [1 ]
Oliva, Rosario [2 ]
Winter, Roland [1 ]
机构：
[1] TU Dortmund Univ, Dept Chem & Chem Biol, Biophys Chem, Otto Hahn Str 4a, D-44227 Dortmund, Germany
[2] Univ Naples Federico II, Dept Chem Sci, Via Cintia 4, I-80126 Naples, Italy
来源：
PHYSICAL CHEMISTRY CHEMICAL PHYSICS | 2023年 / 25卷 / 16期
关键词：
INFRARED-SPECTROSCOPY; HYDROSTATIC-PRESSURE; FT-IR; PHOSPHATIDYLETHANOLAMINE; MODEL; INACTIVATION; MISCIBILITY; DYNAMICS; BILAYERS; PROTEIN;
D O I：
10.1039/d3cp00560g
中图分类号：
O64 [物理化学（理论化学）、化学物理学];
学科分类号：
070304 ; 081704 ;
摘要：
The helical structure that cationic antimicrobial peptides (cAMPs) adopt upon interaction with membranes is key to their activity. We show that a high hydrostatic pressure not only increases the propensity of cAMPs to adopt a helical conformation in the presence of bacterial lipid bilayer membranes, but also in bulk solution, and the effect on bacterial membranes persists even up to 10 kbar. Therefore, high-pressure treatment could boost cAMP activity in high-pressure food processing to extend the shelf-life of food.
引用
收藏
页码：11185 / 11191
页数：7
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