A physicochemical and conformational study of co-solvent effect on the molecular interactions between similarly charged protein surfactant (BSA-SDBS) system

Sharma, Vivek; Yáñez, Osvaldo; Alegría-Arcos, Melissa; Kumar, Ashish; Thakur, Ramesh; Cantero-López, Plinio

doi:10.1016/j.jct.2019.106022

Cited by 35 publications

(9 citation statements)

References 49 publications

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“…First of all, an increase in the amount of [B(Ph) 4 ] − in the system has no impact on the position of an initial strong emission band of tryptophan residues in BSA at approximately 348 nm. Secondly, it can be observed that the intrinsic fluorescence intensity of the albumin (free and saturated with [B(Ph) 4 ] − ) decreases regularly with the addition of SDS, accompanied by a significant blue shift from 348 nm to 332 nm, which may be a result of conformational changes in the BSA structure under the action of the surfactant (exposure of tryptophan residues to a more hydrophobic environment) [24]. Furthermore, the higher the amount of [B(Ph) 4 ] − ions in the mixture, the lower the changes in the fluorescence intensity of BSA under the action of SDS.…”

Section: Steady-state Fluorescence Spectroscopymentioning

confidence: 99%

Effect of Tetraphenylborate on Physicochemical Properties of Bovine Serum Albumin

et al. 2021

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The binding interactions of bovine serum albumin (BSA) with tetraphenylborate ions ([B(Ph)4]−) have been investigated by a set of experimental methods (isothermal titration calorimetry, steady-state fluorescence spectroscopy, differential scanning calorimetry and circular dichroism spectroscopy) and molecular dynamics-based computational approaches. Two sets of structurally distinctive binding sites in BSA were found under the experimental conditions (10 mM cacodylate buffer, pH 7, 298.15 K). The obtained results, supported by the competitive interactions experiments of SDS with [B(Ph)4]− for BSA, enabled us to find the potential binding sites in BSA. The first site is located in the subdomain I A of the protein and binds two [B(Ph)4]− ions (logK(ITC)1 = 7.09 ± 0.10; ΔG(ITC)1 = −9.67 ± 0.14 kcal mol−1; ΔH(ITC)1 = −3.14 ± 0.12 kcal mol−1; TΔS(ITC)1 = −6.53 kcal mol−1), whereas the second site is localized in the subdomain III A and binds five ions (logK(ITC)2 = 5.39 ± 0.06; ΔG(ITC)2 = −7.35 ± 0.09 kcal mol−1; ΔH(ITC)2 = 4.00 ± 0.14 kcal mol−1; TΔS(ITC)2 = 11.3 kcal mol−1). The formation of the {[B(Ph)4]−}–BSA complex results in an increase in the thermal stability of the alfa-helical content, correlating with the saturation of the particular BSA binding sites, thus hindering its thermal unfolding.

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Section: Steady-state Fluorescence Spectroscopymentioning

confidence: 99%

Effect of Tetraphenylborate on Physicochemical Properties of Bovine Serum Albumin

et al. 2021

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“…The observed shift and alteration in the fluorescence intensity of the attained band provide essential information about events that affect the microenvironment surrounding the aromatic residues in the protein molecule (such as protein conformational transitions, ligand binding, denaturation, etc.) [ 48 ] and may be a result of conformational changes in BSA structure, which lead to the exposure of intrinsic fluorophores to more hydrophobic environment (the change in the environment of tryptophan and an increase in hydrophobicity in the vicinity of this residue due to the presence of the alkyl chains of the surfactant molecules) [ 49 ]. On the other hand, at pH 7.4, anionic D and E residues remain near W 134 , which lies at the surface of BSA (subdomain IB) [ 50 ].…”

Section: Resultsmentioning

confidence: 99%

“…It has been reported that the positive Δ H and Δ S values are associated with hydrophobic interactions playing a major role in the binding reaction; negative Δ H and Δ S values are correlated with van der Walls interactions and hydrogen bonding, while electrostatic forces usually make Δ H ≈ 0 or Δ H < 0 and Δ S > 0 [ 89 ]. The negative sign for free energy change of quenching ΔG (

) for all studied surfactants indicates the spontaneity of their binding with bovine serum albumin in the concentration range employed [ 49 ]. The positive Δ H (12.1 kJ mol −1 for pH 5.0 and 9.23 kJ mol −1 for pH 7.0) and Δ S (75.1 J mol −1 K −1 for pH 5.0 and 70.0 J mol −1 K −1 for pH 7.0) indicate that the interaction between BSA and CPC is mainly entropy-driven, the enthalpy is unfavorable for it, and the hydrophobic forces play a major role with less dominating hydrogen bonds formation.…”

Section: Resultsmentioning

confidence: 99%

On the Effect of pH, Temperature, and Surfactant Structure on Bovine Serum Albumin–Cationic/Anionic/Nonionic Surfactants Interactions in Cacodylate Buffer–Fluorescence Quenching Studies Supported by UV Spectrophotometry and CD Spectroscopy

Żamojć

Wyrzykowski

Chmurzyński

2021

IJMS

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Due to the fact that surfactant molecules are known to alter the structure (and consequently the function) of a protein, protein–surfactant interactions are very important in the biological, pharmaceutical, and cosmetic industries. Although there are numerous studies on the interactions of albumins with surfactants, the investigations are often performed at fixed environmental conditions and limited to separate surface-active agents and consequently do not present an appropriate comparison between their different types and structures. In the present paper, the interactions between selected cationic, anionic, and nonionic surfactants, namely hexadecylpyridinium chloride (CPC), hexadecyltrimethylammonium bromide (CTAB), sodium dodecyl sulfate (SDS), polyethylene glycol sorbitan monolaurate, monopalmitate, and monooleate (TWEEN 20, TWEEN 40, and TWEEN 80, respectively) with bovine serum albumin (BSA) were studied qualitatively and quantitatively in an aqueous solution (10 mM cacodylate buffer; pH 5.0 and 7.0) by steady-state fluorescence spectroscopy supported by UV spectrophotometry and CD spectroscopy. Since in the case of all studied systems, the fluorescence intensity of BSA decreased regularly and significantly under the action of the surfactants added, the fluorescence quenching mechanism was analyzed thoroughly with the use of the Stern–Volmer equation (and its modification) and attributed to the formation of BSA–surfactant complexes. The binding efficiency and mode of interactions were evaluated among others by the determination, comparison, and discussion of the values of binding (association) constants of the newly formed complexes and the corresponding thermodynamic parameters (ΔG, ΔH, ΔS). Furthermore, the influence of the structure of the chosen surfactants (charge of hydrophilic head and length of hydrophobic chain) as well as different environmental conditions (pH, temperature) on the binding mode and the strength of the interaction has been investigated and elucidated.

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“…For example water extracted from mango leaves in the presence of SDS have been used for the removal of Cr(IV) from contaminated effluents [80]. From the last many years surfactants have been used in drug delivery where they act as drug carriers for the transportation of hydrophobic drugs [81][82][83]. Hydrophobic dextranes are considered as best carriers based on their biodegradable nature.…”

Section: Applications Of Surfactants In Various Fieldsmentioning

confidence: 99%

Application of surfactants for better tomorrow

Fatma

Sharma²,

Kumar

2022

J. Phys.: Conf. Ser.

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Surfactants are the important class of amphiphilic species, which consists of both hydrophilic as well as hydrophobic part. They are characterized by some important properties like critical micelle concentration (CMC), charge, hydrophile-lypophile balance (HLB), aggregation, and chemical structure, which make them good emulsifying, dispersing and foaming agents. Presently, the global demand of the surfactants is on the peak due to their increased applications in detergents, paints, food emulsion, biotechnological processes, biosciences, pharmaceuticals, cosmetic products, etc. In order to prevent Corona pandemic disease, WHO and other regulatory authorities have recommended frequent use of soaps and sanitizers that makes surfactants an important class of species to be explored more in terms of their applications.

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A physicochemical and conformational study of co-solvent effect on the molecular interactions between similarly charged protein surfactant (BSA-SDBS) system

Cited by 35 publications

References 49 publications

Effect of Tetraphenylborate on Physicochemical Properties of Bovine Serum Albumin

Effect of Tetraphenylborate on Physicochemical Properties of Bovine Serum Albumin

On the Effect of pH, Temperature, and Surfactant Structure on Bovine Serum Albumin–Cationic/Anionic/Nonionic Surfactants Interactions in Cacodylate Buffer–Fluorescence Quenching Studies Supported by UV Spectrophotometry and CD Spectroscopy

Application of surfactants for better tomorrow

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