Binding of Triton X-100 to bovine serum albumin as studied by surface tension measurements

Tribout, Marianne; Paredes, Sergio; González-Mañas, Juan Manuel; Goñi, Félix Lix M F.M.

doi:10.1016/0165-022x(91)90025-r

Cited by 20 publications

(15 citation statements)

References 5 publications

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“…Much research has been devoted to protein interactions with conventional surfactants such as N , N , N ‐trimethyl‐1‐hexadecanaminium bromide (CTAB), sodium dodecyl sulphate (SDS) and 2‐[4‐(2,4,4‐trimethylpentan‐2‐yl)phenoxy]ethanol (Triton X‐100) but less information is known about Gemini protein surfactant interactions . ‘Gemini surfactant’ is a name given to a family of synthetic amphiphiles possessing, in sequence, a long hydrocarbon chain, an ionic group, a spacer, a second ionic group, and another hydrocarbon tail.…”

Section: Introductionmentioning

confidence: 99%

Spectroscopic and molecular modelling analysis of the interaction between ethane‐1,2‐diyl bis(N,N‐dimethyl‐N‐hexadecylammoniumacetoxy)dichloride and bovine serum albumin

et al. 2015

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Several spectroscopic approaches namely fluorescence, time-resolved fluorescence, UV-visible, and Fourier transform infra-red (FT-IR) spectroscopy were employed to examine the interaction between ethane-1,2-diyl bis(N,N-dimethyl-N-hexadecylammoniumacetoxy)dichloride (16-E2-16) and bovine serum albumin (BSA). Fluorescence studies revealed that 16-E2-16 quenched the BSA fluorescence through a static quenching mechanism, which was further confirmed by UV-visible and time-resolved fluorescence spectroscopy. In addition, the binding constant and the number of binding sites were also calculated. The thermodynamic parameters at different temperatures (298 K, 303 K, 308 K and 313 K) indicated that 16-E2-16 binding to BSA is entropy driven and that the major driving forces are electrostatic interactions. Decrease of the α-helix from 53.90 to 46.20% with an increase in random structure from 22.56 to 30.61% were also observed by FT-IR. Furthermore, the molecular docking results revealed that 16-E2-16 binds predominantly by electrostatic and hydrophobic forces to some residues in the BSA sub-domains IIA and IIIA.

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Section: Introductionmentioning

confidence: 99%

Spectroscopic and molecular modelling analysis of the interaction between ethane‐1,2‐diyl bis(N,N‐dimethyl‐N‐hexadecylammoniumacetoxy)dichloride and bovine serum albumin

et al. 2015

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“…The ␣-helices of each subdomain line a number of hydrophobic cavities, some of which have been shown to serve as binding pockets for myristate (Curry et al, 1998) and other ligands, particularly in subdomains IIA and IIIA (He and Carter, 1992;Carter and Ho, 1994). Binding data obtained with detergents have shown that serum albumin interacts with Triton X-100 (Makino et al, 1973;Sukow et al, 1980;Tribout et al, 1991), deoxycholate (Makino et al, 1973), and ␤-octylglucoside (Wasylewski and Kozik, 1979) at a large number of sites, but the relation of this binding compared with that of other ligands is unknown.…”

Section: Introductionmentioning

confidence: 99%

Detergents as Probes of Hydrophobic Binding Cavities in Serum Albumin and Other Water-Soluble Proteins

Kragh‐Hansen

Hellec

Foresta

et al. 2001

Biophysical Journal

104

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As an extension of our studies on the interaction of detergents with membranes and membrane proteins, we have investigated their binding to water-soluble proteins. Anionic aliphatic compounds (dodecanoate and dodecylsulfate) were bound to serum albumin with high affinity at nine sites; related nonionic detergents (C12E8 and dodecylmaltoside) were bound at seven to eight sites, many in common with those of dodecanoate. The compounds were also bound in the hydrophobic cavity of beta-lactoglobulin, but not to ovalbumin. In addition to the generally recognized role of the Sudlow binding region II of serum albumin (localized at the IIIA subdomain) in fatty acid binding, quenching of the fluorescence intensity of tryptophan-214 by 7,8-dibromododecylmaltoside and 12-bromododecanoate also implicate the Sudlow binding region I (subdomain IIA) as a locus for binding of aliphatic compounds. Our data document the usefulness of dodecyl amphipathic compounds as probes of hydrophobic cavities in water-soluble proteins. In conjunction with recent x-ray diffraction analyses of fatty acid binding as the starting point we propose a new symmetrical binding model for the location of nine high-affinity sites on serum albumin for aliphatic compounds.

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“…Wool and human hair are proteinacious in nature, which on a regular basis are exposed to surfactants. The single-chain surfactants including cetyltrimethylammonium bromide (CTAB), SDS, and tertcetylphenoxypolyethoxyethanol (Triton X-100) are investigated extensively [65][66][67][68][69] and proteins with double-chain surfactants interactions are studied less. The interactions between nonionic water-soluble polymers and surfactants are of technological importance and have been the subject of intense studies over the last three decades due to their wide range of applications [70].…”

Section: Nonionic Surfactantsmentioning

confidence: 99%

Surfactant–Amino Acid and Surfactant–Surfactant Interactions in Aqueous Medium: a Review

Malik

2015

Appl Biochem Biotechnol

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An overview of surfactant-amino acid interactions mainly in aqueous medium has been discussed. Main emphasis has been on the solution thermodynamics and solute-solvent interactions. Almost all available data on the topic has been presented in a lucid and simple way. Conventional surfactants have been discussed as amphiphiles forming micelles and amino acids as additives and their effect on the various physicochemical properties of these conventional surfactants. Surfactant-surfactant interactions in aqueous medium, various mixed surfactant models, are also highlighted to assess their interactions in aqueous medium. Finally, their applied part has been taken into consideration to interpret their possible uses.

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Binding of Triton X-100 to bovine serum albumin as studied by surface tension measurements

Cited by 20 publications

References 5 publications

Spectroscopic and molecular modelling analysis of the interaction between ethane‐1,2‐diyl bis(N,N‐dimethyl‐N‐hexadecylammoniumacetoxy)dichloride and bovine serum albumin

Spectroscopic and molecular modelling analysis of the interaction between ethane‐1,2‐diyl bis(N,N‐dimethyl‐N‐hexadecylammoniumacetoxy)dichloride and bovine serum albumin

Detergents as Probes of Hydrophobic Binding Cavities in Serum Albumin and Other Water-Soluble Proteins

Surfactant–Amino Acid and Surfactant–Surfactant Interactions in Aqueous Medium: a Review

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