Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/46437

TitlePhysicochemical study of biomolecular interactions between lysosomotropic surfactants and bovine serum albumin
Author(s)Janek, Tomasz
Czyznikowska, Zaneta
Luczynski, Jacek
Gudiña, Eduardo J.
Rodrigues, L. R.
Galezowska, Joanna
KeywordsLysosomotropic substances
Surface tension
Density functional theory
Fluorescence quenching
Circular dichroism
Isothermal titration calorimetry
Issue dateNov-2017
PublisherElsevier
JournalColloids and Surfaces B: Biointerfaces
CitationJanek, Tomasz; Czyznikowska, Zaneta; Luczynski, Jacek; Gudiña, Eduardo J.; Rodrigues, Lígia R.; Galezowska, Joanna, Physicochemical study of biomolecular interactions between lysosomotropic surfactants and bovine serum albumin. Colloids and Surfaces B: Biointerfaces, 159, 750-758, 2017
Abstract(s)The interactions between two cationic lysosomotropic surfactants (2-dodecanoyloxyethyl)trimethylammonium bromide (DMM-11) and (2-dodecanoyloxypropyl)trimethylammonium bromide (DMPM-11) with bovine serum albumin (BSA) in Hepes buffer (pH = 7.4) were systematically studied by surface tension, fluorescence and circular dichroism (CD) spectroscopy and isothermal titration calorimetry (ITC). Furthermore, the size of the micellar aggregates and the polydispersity indexes of both cationic surfactants were studied by dynamic light scattering technique (DLS). The hydrodynamic radii, micellar volumes and aggregation numbers were calculated using a method based on density functional theory (DFT). The results showed that, in both cases, the surface tension was modified upon addition of BSA, and the critical micelle concentration (CMC) values of DMM-11 and DMPM-11 were higher in the presence of BSA. The fluorescence intensity of BSA decreased significantly as the concentration of both cationic surfactants increased and this effect was attributed to the formation of surfactant-BSA complexes. Synchronous fluorescence spectrometry showed the binding-induced conformational changes in BSA. Finally, CD and DLS results revealed the occurrence of changes in the secondary structure of the protein in the presence of both surfactants. In conclusion, understanding the interactions between lysosomotropic surfactants and BSA is required to explore their potential applications in medicine.
TypeArticle
URIhttp://hdl.handle.net/1822/46437
DOI10.1016/j.colsurfb.2017.08.046
ISSN0927-7765
Publisher versionhttp://www.journals.elsevier.com/colloids-and-surfaces-b-biointerfaces/
Peer-Reviewedyes
AccessOpen access
Appears in Collections:CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series

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