Utilize este identificador para referenciar este registo:
https://hdl.handle.net/1822/46437
Título: | Physicochemical study of biomolecular interactions between lysosomotropic surfactants and bovine serum albumin |
Autor(es): | Janek, Tomasz Czyznikowska, Zaneta Luczynski, Jacek Gudiña, Eduardo J. Rodrigues, L. R. Galezowska, Joanna |
Palavras-chave: | Lysosomotropic substances Surface tension Density functional theory Fluorescence quenching Circular dichroism Isothermal titration calorimetry |
Data: | Nov-2017 |
Editora: | Elsevier 1 |
Revista: | Colloids and Surfaces B: Biointerfaces |
Citação: | Janek, 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 |
Resumo(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. |
Tipo: | Artigo |
URI: | https://hdl.handle.net/1822/46437 |
DOI: | 10.1016/j.colsurfb.2017.08.046 |
ISSN: | 0927-7765 |
Versão da editora: | http://www.journals.elsevier.com/colloids-and-surfaces-b-biointerfaces/ |
Arbitragem científica: | yes |
Acesso: | Acesso aberto |
Aparece nas coleções: | CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series |
Ficheiros deste registo:
Ficheiro | Descrição | Tamanho | Formato | |
---|---|---|---|---|
document_46953_1.pdf | 2,72 MB | Adobe PDF | Ver/Abrir |