: 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.

High pressure treatment promotes the deteriorating effect of cationic antimicrobial peptides on bacterial membranes / Kriegler, S.; Jaworek, M. W.; Oliva, R.; Winter, R.. - In: PHYSICAL CHEMISTRY CHEMICAL PHYSICS. - ISSN 1463-9076. - 25:16(2023), pp. 11185-11191. [10.1039/d3cp00560g]

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

Oliva, R.
;
2023

Abstract

: 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.
2023
High pressure treatment promotes the deteriorating effect of cationic antimicrobial peptides on bacterial membranes / Kriegler, S.; Jaworek, M. W.; Oliva, R.; Winter, R.. - In: PHYSICAL CHEMISTRY CHEMICAL PHYSICS. - ISSN 1463-9076. - 25:16(2023), pp. 11185-11191. [10.1039/d3cp00560g]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/938286
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