The Binding of Divers Detergent Anions to Bovine Serum Albumin<sup>*</sup>

Reynolds, Jacqueline A.; Herbert, Sarah; Polet, Helga; Steinhardt, Jacinto

doi:10.1021/bi00855a038

Cited by 297 publications

(169 citation statements)

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“…This anionic compound, which is generally considered a potent denaturant [4], was investigated in many early works on bovine serum albumin (BSA) [5][6][7][8][9][10] and a number of other proteins [11][12][13][14][15][16][17]. This led to several general conclusions regarding the modes of interaction of SDS and proteins (for reviews see [18][19][20]).…”

mentioning

confidence: 99%

Glycoprotein-surfactant interactions: A calorimetric and spectroscopic investigation of the phytase-SDS system

Bagger

Hoffmann

Fuglsang

et al. 2007

Biophysical Chemistry

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This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT2 AbstractThe interactions of sodium dodecyl sulfate (SDS) and two glyco-variants of the enzyme phytase from Peniophora lycii were investigated. One variant (Phy) was heavily glycosylated while the other (dgPhy) was enzymatically deglycosylated. Effects at 24°C of titrating SDS to Phy and dgPhy were studied by Isothermal Titration Calorimetry (ITC) and Synchrotron Radiation Circular Dichroism (SRCD) spectroscopy. Comparisons of results for the two variants were used to elucidate glycan-surfactant interrelationships.The CD spectra suggested that both the native and the SDS-denatured states of the two variants were mutually similar, and hence that the denaturation process was structurally equivalent for the two glyco-variants.The denatured state was far from fully unfolded and probably retained a substantial content of native-like structure. Furthermore, it was found that the glycans brought about only a small increase in the resistance towards SDS induced denaturation. The SDS concentration required to denature half of the protein molecules differed less than 1 mM for the two variants.The affinity for SDS of both variants was unusually low. The amount of bound SDS (w/w) at different stages of the binding isotherm was 3-10 times lower than that reported for the most previously investigated globular proteins. Analysis of the relative affinity of the glycan and peptide moieties suggested that the carbohydrates bind much less surfactant. At saturation, glycans adsorbed about half as much SDS (in g/g) as the peptide moiety of Phy and about five times less than average proteins.

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confidence: 99%

Glycoprotein-surfactant interactions: A calorimetric and spectroscopic investigation of the phytase-SDS system

Bagger

Hoffmann

Fuglsang

et al. 2007

Biophysical Chemistry

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“…At levels of unbound ligand higher than 60-65 mM, albumin is saturated with decylsulfate. The binding ratio (5 = 110) is higher than that reported by Reynolds et al [3] for bovine serum albumin (V = 27), and also for that of human serum albumin (V = 25) as obtained by Steinhardt et al [14]. The results cited are based on equilibrium dialysis data at pH 5.6 ( I = 0.033 M).…”

Section: Binding Isothermsmentioning

confidence: 57%

“…The first 10-11 octylsulfate molecules are bound on different binding sites (areas) on the albumin molecule. The saturation of these binding sites is probably associated with a conformational change of the albumin molecule [2,3]. This conformational change is not detectable by viscosity (Fig.…”

Section: Discussionmentioning

confidence: 94%

“…Only a very small increase in ysp/c is observed at high concentrations of free octylsulfate, and it is thus apparent that binding of octylsulfate does not cause a measurable change of the conformation of albumin. However, binding of both decylsulfate and dodecylsulfate below the critical micellar concentration results in the kind of viscosity change which is characteristic for unfolding of albumin [3]. The viscosity of the decylsulfate-albumin complexes is drastically increased at concentrations of free ligand above 10-15 mM and the curve exhibits a flattening off in the region 60-80 mM.…”

Section: Viscositymentioning

confidence: 99%

“…The number of molecules bound per protein molecule, the association constants and the cooperativity have mainly been determined by equilibrium dialysis [2-51. The conformational changes occurring at high binding levels and during unfolding have been characterized by optical rotatory dispersion [2,3], viscosity [3,4] and gel chromatography [6,7].…”

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confidence: 99%

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Complexes of Aliphatic Sulfates and Human-Serum Albumin Studied by 13C Nuclear-Magnetic-Resonance Spectroscopy

Kragh‐Hansen

Riisom²

1976

Eur J Biochem

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The interaction of human serum albumin and various long-chain sulfates has been studied. Binding of sodium octylsulfate to albumin increases in the concentration range studied as measured by equilibrium dialysis. In contrast, binding of the sodium salts of decylsulfate and dodecylsulfate is constant at a concentration of free ligand higher than SO mM and 12 mM corresponding to binding of 110 and 83 sulfate molecules per albumin molecule, respectively. Viscosity measurements indicate that binding of decylsulfate and dodecylsulfate is associated with unfolding of the albumin molecule. In contrast, binding of octylsulfate does not cause gross conformation changes of albumin.However, the chemical shifts of bound octylsulfate obtained by natural abundance 13C nuclear magnetic resonance spectroscopy show significant changes at 80 mM and 150 mM free ligand. The spin-spin and spin-lattice relaxation times also show changes in the association between octylsulfate and albumin at 80 mM free sulfate. These observations indicate alterations in the binding properties at 10 -11 and 20 -21 bound ligand molecules, respectively.The relaxation times are considerably increased by binding to albumin, indicating less motional freedom of the molecules in the bound state. At high levels of sulfate binding the relaxation times of the terminal methyl group approach that of free ligand. The chemical shifts of all the bound carbon atoms studied, except the CH2 group nearest to the sulfate group (Cl), are comparable to those observed in the micellar state indicating binding in a non-polar environment. However, the relaxation times indicate that the motional freedom of sulfates bound to albumin is much more restricted than in micelles. The shift of C1 indicates that this part of the ligand is situated in a polar environment.The following model for binding of high concentrations of aliphatic detergents is proposed. The sulfate group and the CH2 group nearest to it is situated in a polar medium caused by interaction between the sulfate group and a positive amino acid residue on albumin. The other CH2 groups interact with hydrophobic amino acid residues on albumin. The CH3 group does not interact with the albumin molecule but associates with other methyl groups of sulfates bound in the vicinity forming a hydrophobic medium.Albumin is able to bind a great number of different small molecules with a high affinity, among them being aliphatic sulfates [l]. To elucidate the nature of the complexes between, for example, sodium dodecylsulfate and albumin several techniques have been used. The number of molecules bound per protein molecule, the association constants and the cooperativity have mainly been determined by equilibrium dialysis [2-51. The conformational changes occurring at high binding levels and during unfolding have been characterized by optical rotatory dispersion [2,3], viscosity [3,4] and gel chromatography [6,7].Abbreviations. NMR, nuclear magnetic resonance; C,, C atom number n counted from the polar end of the sulfates.A few studie...

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Amphipathic polymers with stimuli-responsive microdomains for water remediation: Binding studies withp-cresol

Richardson

Armentrout

McCormick

1999

J. Appl. Polym. Sci.

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Amphipathic, stimuli-responsive water-soluble polymers have been investigated as potential remediation agents for micellar enhanced ultrafiltration (MEUF). The systems represent divergent architectural types, a triblock ABA copolymer of PEO-PPO-PEO, an n-octylamide modified poly(sodium maleate-alt-ethyl vinyl ether), and the transport protein, bovine serum albumin. Each type exhibits stimuli-dependent microphase separation or domain formation in response to temperature, pH, and/or ionic strength changes. Segmental associations result in hydrophobic clusters resembling those present in small molecule surfactant micelles. The effects of such segmental aggregation on sequestration of a model hydrophobic foulant, p-cresol, have been investigated using equilibrium dialysis. The favorable molar binding values, the large hydrodynamic dimensions of the stable polymer aggregates, and potential reversibility of foulant loading could have commercial utility in high flow rate, multiple-pass remediation processes.

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The Binding of Divers Detergent Anions to Bovine Serum Albumin^*

Cited by 297 publications

References 14 publications

Glycoprotein-surfactant interactions: A calorimetric and spectroscopic investigation of the phytase-SDS system

Glycoprotein-surfactant interactions: A calorimetric and spectroscopic investigation of the phytase-SDS system

Complexes of Aliphatic Sulfates and Human-Serum Albumin Studied by 13C Nuclear-Magnetic-Resonance Spectroscopy

Amphipathic polymers with stimuli-responsive microdomains for water remediation: Binding studies withp-cresol

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The Binding of Divers Detergent Anions to Bovine Serum Albumin*

Cited by 297 publications

References 14 publications

Glycoprotein-surfactant interactions: A calorimetric and spectroscopic investigation of the phytase-SDS system

Glycoprotein-surfactant interactions: A calorimetric and spectroscopic investigation of the phytase-SDS system

Complexes of Aliphatic Sulfates and Human-Serum Albumin Studied by 13C Nuclear-Magnetic-Resonance Spectroscopy

Amphipathic polymers with stimuli-responsive microdomains for water remediation: Binding studies withp-cresol

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The Binding of Divers Detergent Anions to Bovine Serum Albumin^*