Small-angle X-ray scattering and electron paramagnetic resonance study of the interaction of bovine serum albumin with ionic surfactants

Gelamo, Émerson Luíz; Itri, Rosângela; Alonso, Antônio; Silva, Junaine Vasques da; Tabak, Marcel

doi:10.1016/j.jcis.2004.04.065

Cited by 90 publications

(90 citation statements)

References 35 publications

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“…To use them correctly, it is necessary to have an idea of how and in which amounts they interact with proteins. Although surfactant-protein interactions have been widely studied for half a century [1][2][3][4][5], the mechanism of interaction is not well understood. Knowledge of the interactions is not only fundamental in theoretics, but also practical in industrial applications.…”

Section: Introductionmentioning

confidence: 99%

Interaction of bovine serum albumi with two alkylimidazolium-based ionic liquids investigated by microcalorimetry and circular dichroism

Zhu¹,

Li²,

Zheng³

2011

JBPC

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The interactions of bovine serum albumin (BSA) with two alkylimidazolium-based ionic liquids, 1-butyl-3-methylimidazolium tetrafluoroborate ([bmim]BF 4 ) and 1-butyl-3-methylimidazolium hexafluorophosphate ([bmim]PF 6 ), in buffer solutions at pH 7.0 were investigated by isothermal titration calorimetry (ITC) and circular dichroism (CD). CD spectra showed that the two ionic liquids changed the secondary structure of BSA. Data process was based on the supposition that there were several independent types of binding sites on each BSA molecule for the two ligand molecules. The results obtained by using this supposition combined with Langmuir adsorption model showed that there were two types of such binding sites. One was the high affinity binding site, and the other was the low affinity binding site. The binding constants, changes in enthalpy, entropy and Gibbs free energy for the two types of binding were obtained, which showed that the two types of binding were driven by a favorable entropy increase. Furthermore, for either the ionic liquids, the number of the high affinity binding sites is much smaller than that of the low affinity ones. These results were interpreted with the molecular structure of BSA and the different substituent groups on imidazole ring of the two ionic liquid molecules.

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Section: Introductionmentioning

confidence: 99%

Interaction of bovine serum albumi with two alkylimidazolium-based ionic liquids investigated by microcalorimetry and circular dichroism

Zhu¹,

Li²,

Zheng³

2011

JBPC

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“…In this site of crystallized HSA, a cluster of positive charges including Arg218 and Arg222 exists [16,17,18]. Data of neutron [21] and X-ray small-angle scattering [22] show that size of HSA molecule is similar in crystals and solutions; perhaps, the site I structure is similar as well. So, it can be suggested that negatively charged carboxyl of CAPIDAN binds with Arg218 or Arg222 of the site I, and nitrate suppresses this interaction.…”

Section: Discussionmentioning

confidence: 99%

Nitrate Anion as a Probe for Electrostatic Interactions in Complexes Protein-Ligand

Смолина¹,

Dobretsov²,

Syrejshchikova³

et al. 2013

EJB

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(Smolina N. V.), gdobretsov@newmail.ru(Dobretsov G. E.), syrej@sci.lebedev.ru(Syrejshchikova T. I.), varvara-bf@list.ru (Kalinina V. V.) To cite this article: Abstract: We are proposing a new technique for studying interaction of charged biomolecules. It is based on a difference between nitrate and chloride anion influence on electrostatic interactions in order to detect the role of positively charged guanidine groups of proteins. This comparison was demonstrated for human serum albumin (HSA) interaction with a fluorescent reporter, CAPIDAN. Nitrate anions lower their binding constant (K). There are two causes that are responsible for that K decrease induced by nitrate. The first, rise of the ionic strength (like to chloride), and the second, a specific one: at the same concentration and ionic strength nitrate anion more significantly lowers K than chloride anion. The study of electric conductivity of chloride and nitrate salts shows that nitrate anions better than chloride anions form complexes with guanidine cations. Therefore it can be assumed that the nitrate-chloride techniques detect a direct contact of negatively charged carboxyl of CAPIDAN with positively charged arginine residues of HSA. HSA site I includes Arg 218 and Arg 222. It is possible that the CAPIDAN carboxyl binds to one of these arginines.

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“…There are several experimental methods available for determination of protein secondary structure, such as circular dichroism (CD) (Shanmugam & Polavarapu, 2006), nuclear magnetic resonance (NMR) , X-ray scattering and diffraction , calorimetry and fluorescence (Gelamo et al, 2002), diffuse reflectance (DR) (Ishida & Griffiths, 1993), electron paramagnetic resonance ESR (Gelamo et al, 2004), Raman (Bolton & Scherer, 1989), near infrared (NIR) (Wu et al, 2000) and IR spectroscopy (Cai & Singh, 1999;Grdadolnik & Maréchal, 2001a& 2001bJackson et al, 1989;Maréchal, 2004Maréchal, & 2003van de Weert et al, 2001;Zhang & Yan, 2005). The last has for many years been a promising technique for the determination of the secondary structure of proteins in that some peptide vibrations are sensitive to conformation (Harris & Chapman, 1992;Jackson & Mantsch, 1995).…”

Section: Proteinsmentioning

confidence: 99%

Specific Applications of Vibrational Spectroscopy in Biomedical Engineering

Olsztyńska-Janus¹,

Gąsior-Głogowska²,

Szymborska-Małek³

et al. 2011

Biomedical Engineering, Trends, Research and Technologies

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Small-angle X-ray scattering and electron paramagnetic resonance study of the interaction of bovine serum albumin with ionic surfactants

Cited by 90 publications

References 35 publications

Interaction of bovine serum albumi with two alkylimidazolium-based ionic liquids investigated by microcalorimetry and circular dichroism

Interaction of bovine serum albumi with two alkylimidazolium-based ionic liquids investigated by microcalorimetry and circular dichroism

Nitrate Anion as a Probe for Electrostatic Interactions in Complexes Protein-Ligand

Specific Applications of Vibrational Spectroscopy in Biomedical Engineering

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