Lack of Association between a Cationic Protein and a Cationic Fluorosurfactant
2007 (English)In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 23, no 2, 771-775 p.Article in journal (Refereed) Published
Surface tension, F-19 and H-1 NMR spectroscopy, and cryotransmission electron microscopy are used to characterize the state of association in aqueous solutions of a fluorosurfactant CF3(CF2)(n)SO2NH(CH2)(3-4)N(CH3)(3)(+) I- (n = 8, 6) with and without lysozyme added. In the absence of lysozyme, we find monomers, small aggregates, and large vesicles to coexist, with the individual fluorosurfactant molecules exchanging slowly (> 1 ms) among those states. When both lysozyme and fluorosurfactant are present in the solution, they have no measurable influence on the physical state of the other. In contrast, a hydrogenated cationic surfactant with the same headgroup, hexadecyltrimethylammonium bromide, is shown to associate to lysozyme.
Place, publisher, year, edition, pages
2007. Vol. 23, no 2, 771-775 p.
Ionic surfactant, Physicochemical properties, Enzyme, Hydrolases, Glycosidases, O-Glycosidases, Electrochemistry, Cationic surfactant, Vesicle, Aggregate, Monomer, Lysozyme, Aqueous solution, Electron spectrometry, NMR spectrometry, Surface tension, Protein, Association
IdentifiersURN: urn:nbn:se:uu:diva-24300DOI: 10.1021/la062469zISI: 000243338500061PubMedID: 17209632OAI: oai:DiVA.org:uu-24300DiVA: diva2:52074