High pressure treatment promotes the deteriorating effect of cationic antimicrobial peptides on bacterial membranes
dc.contributor.author | Kriegler, Simon | |
dc.contributor.author | Jaworek, Michel W. | |
dc.contributor.author | Oliva, Rosario | |
dc.contributor.author | Winter, Roland | |
dc.date.accessioned | 2024-07-08T12:59:11Z | |
dc.date.available | 2024-07-08T12:59:11Z | |
dc.date.issued | 2023-03-29 | |
dc.description.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. | en |
dc.identifier.uri | http://hdl.handle.net/2003/42587 | |
dc.identifier.uri | http://dx.doi.org/10.17877/DE290R-24422 | |
dc.language.iso | en | de |
dc.relation.ispartofseries | Physical chemistry, chemical physics;25(16) | |
dc.rights.uri | https://creativecommons.org/licenses/by/3.0/ | |
dc.subject.ddc | 540 | |
dc.title | High pressure treatment promotes the deteriorating effect of cationic antimicrobial peptides on bacterial membranes | en |
dc.type | Text | de |
dc.type.publicationtype | Article | de |
dcterms.accessRights | open access | |
eldorado.secondarypublication | true | de |
eldorado.secondarypublication.primarycitation | Phys. Chem. Chem. Phys., 2023,25, 11185-11191 | de |
eldorado.secondarypublication.primaryidentifier | https://doi.org/10.1039/D3CP00560G | de |