Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/58393

TitleBiomolecular interactions of lysosomotropic surfactants with cytochrome c and its effect on the protein conformation: A biophysical approach
Author(s)Janek, Tomasz
Czelen, Przemyslaw
Gudiña, Eduardo José
Rodrigues, L. R.
Czyznikowska, Zaneta
KeywordsLysosomotropic surfactant
Cytochrome
Fluorescence quenching
Circular dichroism
Molecular dynamic simulations
Cytochrome c
Issue dateApr-2019
PublisherElsevier
JournalInternational Journal of Biological Macromolecules
CitationJanek, Tomasz; Czelen, Przemyslaw; Gudiña, Eduardo J.; Rodrigues, Lígia R.; Czyznikowska, Zaneta, Biomolecular interactions of lysosomotropic surfactants with cytochrome c and its effect on the protein conformation: A biophysical approach. International Journal of Biological Macromolecules, 126, 1177-1185, 2019
Abstract(s)The molecular interactions between two single-chain lysosomotropic surfactants DMM-11 (2-Dodecanoyloxyethyl)trimethylammonium bromide) and DMPM-11 (2-Dodecanoyloxypropyl)trimethylammonium bromide) with a small heme-protein (cytochrome c (cyt-c)) in Hepes buffer (pH = 7.4) were extensively investigated by surface tension, dynamic light scattering (DLS), circular dichroism (CD) and fluorescence spectroscopy in combination with molecular dynamic simulation techniques. The results demonstrated that surfactants can destroy the hydrophobic cavity of cyt-c, make the α-helical become loose and convert it into the β-sheet structure. The interactions between surfactants and cyt-c are mainly hydrophobic. Molecular modelling approaches were also used to gather a deeper insight on the binding of lysosomotropic surfactants with cyt-c and the in silico results were found to be in good agreement with the experimental ones. This study provides a molecular basis for the applications of protein-surfactant complexes in biological, food, pharmaceutical, industrial and cosmetic systems
TypeArticle
URIhttp://hdl.handle.net/1822/58393
DOI10.1016/j.ijbiomac.2019.01.024
ISSN0141-8130
e-ISSN1879-0003
Publisher versionhttps://www.sciencedirect.com/science/article/pii/S0141813018365012
Peer-Reviewedyes
AccessOpen access
Appears in Collections:CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series

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