Full metadata record
DC FieldValueLanguage
dc.contributor.authorKriegler, Simon-
dc.contributor.authorJaworek, Michel W.-
dc.contributor.authorOliva, Rosario-
dc.contributor.authorWinter, Roland-
dc.date.accessioned2024-07-08T12:59:11Z-
dc.date.available2024-07-08T12:59:11Z-
dc.date.issued2023-03-29-
dc.identifier.urihttp://hdl.handle.net/2003/42587-
dc.identifier.urihttp://dx.doi.org/10.17877/DE290R-24422-
dc.description.abstractThe 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.language.isoende
dc.relation.ispartofseriesPhysical chemistry, chemical physics;25(16)-
dc.rights.urihttps://creativecommons.org/licenses/by/3.0/-
dc.subject.ddc540-
dc.titleHigh pressure treatment promotes the deteriorating effect of cationic antimicrobial peptides on bacterial membranesen
dc.typeTextde
dc.type.publicationtypeArticlede
dcterms.accessRightsopen access-
eldorado.secondarypublicationtruede
eldorado.secondarypublication.primaryidentifierhttps://doi.org/10.1039/D3CP00560Gde
eldorado.secondarypublication.primarycitationPhys. Chem. Chem. Phys., 2023,25, 11185-11191de
Appears in Collections:Physikalische Chemie

Files in This Item:
File Description SizeFormat 
d3cp00560g.pdfDNB960.51 kBAdobe PDFView/Open


This item is protected by original copyright



This item is licensed under a Creative Commons License Creative Commons