Probing peptide–membrane interactions using AFMBrasseur, Robert;Deleu, Magali;Mingeot-Leclercq, Marie-Paule;Francius, Grégory;Dufrêne, Yves(2008) Surface and Interface Analysis — Vol. 40, n° 3-4, p. 151-156 (2008)
Filespdfdocument.pdf Restricted Access Adobe PDF456.31 KBRequest a copyDetailsAuthorsBrasseur, RobertAuthorDeleu, MagaliAuthorMingeot-Leclercq, Marie-PauleUCLouvainAuthorFrancius, GrégoryUCLouvainAuthorDufrêne, YvesUCLouvainAuthorAbstractAtomic force microscopy (AFM) has become a powerful addition to the range of instruments available to probe the organization of lipid monolayers and bilayers. Currently, AFM is the only tool that can provide nanoscale topographic images of supported lipid membranes under physiological conditions, enabling researchers to resolve their detailed structure and to monitor their interaction with drugs, peptides and proteins. Here, we survey recent data obtained by our research groups that demonstrate the power of the technique for exploring peptide–membrane interactions, with an emphasis on microbial lipopeptides and on tilted peptides. Copyright © 2008 John Wiley & Sons, Ltd.Show moreAffiliationsUCLouvainMD/FARM - Ecole de pharmacieUCLouvainSC/CHIM - Département de chimieShow moreCitations APA Chicago FWB Brasseur, R., Deleu, M., Mingeot-Leclercq, M.-P., Francius, G., & Dufrêne, Y. (2008). Probing peptide–membrane interactions using AFM. Surface and Interface Analysis, 40(3-4), 151-156. https://doi.org/10.1002/sia.2682 (Original work published 2008)