Reference : Conformational analyses of bacillomycin D, a natural antimicrobial lipopeptide, alone or...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/129934
Conformational analyses of bacillomycin D, a natural antimicrobial lipopeptide, alone or in interaction with lipid monolayers at the air-water interface
English
Nasir, Mehmet Nail mailto [Université de Liège - ULg > Chimie et bio-industries > Chimie biologique industrielle >]
Besson, Françoise []
Dec-2012
Journal of Colloid & Interface Science
Academic Press
387
1
187-193
Yes (verified by ORBi)
International
0021-9797
1095-7103
Orlando
FL
[en] Bacillomycin D is a natural antimicrobial lipopeptide belonging to the iturin family. It is produced by Bacillus subtilis strains. Bacillomycin D is characterized by its strong antifungal and hemolytic properties, due to its interaction with the plasma membrane of sensitive cells. Until now, only few limited analyses were conducted to understand the biological activities of bacillomycin D at the molecular level. Our purpose was to analyze the conformation of bacillomycin D using IR spectroscopy and to model its interactions with cytoplasmic membranes using Langmuir interfacial monolayers. Our findings indicate that bacillomycin D contains turns and allow to model its three-dimensional structure. Bacillomycin D formed a monolayer film at the air–water interface and kept its turn conformation, as shown by polarization modulation infrared reflection absorption spectroscopy (PM-IRRAS). To identify the membrane lipid target of bacillomycin D, its interactions with pure lipid monolayers were analyzed and an original behavior of the lipopeptide toward cholesterol-containing monolayers was shown. This original behavior was lost when bacillomycin D was interacting with pure cholesteryl acetate monolayers, suggesting the involvement of the alcohol group of cholesterol in the lipopeptide–cholesterol interaction.
Researchers ; Professionals ; Students ; General public ; Others
http://hdl.handle.net/2268/129934

File(s) associated to this reference

Fulltext file(s):

FileCommentaryVersionSizeAccess
Restricted access
JCIS_Nasir.pdfPublisher postprint592.13 kBRequest copy

Bookmark and Share SFX Query

All documents in ORBi are protected by a user license.