Surfactant interactions with biomembranes and proteins

Jones, Malcolm N.

doi:10.1039/cs9922100127

Cited by 357 publications

(252 citation statements)

References 23 publications

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“…The combined analysis of CD and ITC data suggests that both forms of phytase specifically bind 3-4 SDS molecules without detectable changes in the protein structure. This process most likely involves the interaction of the anionic surfactant and cationic groups on the protein, particularly if this binding is located around hydrophobic areas or clefts where the surfactant acyl chain can be lodged [18].…”

Section: Discussionmentioning

confidence: 99%

“…to -10 kJ/mol SDS. Although binding in this affinity range can be measured only approximately at the current protein concentrations, we note that the derived parameters are typical for the specific binding of SDS to proteins [18,41]. As illustrated in the inset of Fig.…”

Section: Accepted M Manuscriptmentioning

confidence: 91%

“…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]). Thus, a certain pattern of binding events has been observed before the adsorption of surfactant eventually reached saturation at about 1.4 g SDS per g protein with reduced S-S bonds [15,21] and somewhat less (~1g/g) in proteins with intact cystines [21].…”

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confidence: 99%

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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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Section: Discussionmentioning

confidence: 99%

Section: Accepted M Manuscriptmentioning

confidence: 91%

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confidence: 99%

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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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“…In our case, the studied protein is a giant multi-oligomeric hemoglobin, and the interaction with surfactant molecules may induce distinct effects such as dissociation at low concentrations and protein denaturation at higher concentrations (25)(26)(27)(28). In this work, the structural conformation of the extracellular hemoglobin of G. paulistus in the oxy-and met-forms in the absence and presence of the anionic SDS surfactant, at pH 7.0 and 9.0, has been studied by means of SAXS to investigate changes produced in the protein structure upon both alkaline dissociation and interaction with the anionic surfactant.…”

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confidence: 99%

Small Angle X-ray Scattering (SAXS) Study of the Extracellular Hemoglobin of Glossoscolex paulistus

Gelamo

Itri

Tabak

2004

Journal of Biological Chemistry

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pH effects on the oligomeric structure of giant Glossoscolex paulistus extracellular hemoglobin in the oxyand met-forms have been studied as well as effects of the addition of anionic sodium dodecyl sulfate surfactant. A radius of gyration of 110 Å is observed for a macromolecule. At 2 mM surfactant, the radius of gyration diminishes slightly for the oxy-form. However, the extrapolated initial scattering intensity (I(0)) decreases a factor of 2.5, indicating protein dissociation. At 20 mM surfactant, further I(0) decrease is observed, with a reduction of radius of gyration to approximately 30 Å consistent with dissociation into smaller subunits. At pH 9.0, the scattering curves are similar to that obtained for the protein in the presence of 20 mM surfactant at pH 7.0. A radius of gyration of approximately 35 Å shows that the giant hemoglobin dissociation into small subunits also occurs at alkaline pH. From the I(0) value, one can suggest that the tetramer is the main scatter at pH 9.0. At pH 7.0, the met-form dissociates to a larger extent at 2 mM surfactant as compared with the oxy-form, and the main scatters seem to be the 1/12 subunit. At pH 9.0, for the oxy-form, the addition of surfactant does not modify the scattering curve and a radius of gyration approximately 30 Å is obtained, while for the met-form some kind of aggregation is observed. Our results give support to conclude that the iron oxidation state is an important factor modulating the oligomeric dissociation.Annelid extracellular hemoglobins are giant molecules that have a characteristic hexagonal bilayer appearence in electron micrographs, high cooperativity of oxygen binding, and low iron and heme contents (1-4). The hemoglobin of the earthworm Lumbricus terrestris (HbLt) 1 is the most extensively studied annelid hemoglobin. It consists of about 180 polypeptide chains in an arrangement of two heme-containing subunits (monomer M and disulfide-bonded trimer T) and non-globin linker subunits with molecular masses in the range 24 -32 kDa. A model of quaternary structure (bracelet model) explains the properties and subunit structure of HbLt: three copies of monomer subunit and three copies of the trimer subunit form a dodecamer subunit, (abcd) 3 of about 200 kDa. Twelve such complexes of heme-containing chains are linked together by 36 heme-deficient linker chains to provide the total mass of about 3500 kDa. The 1/12 subunit of the whole protein is associated then to (abc) 3 d 3 L 3 , where L stands for the linker chains. Since 1996 a significant effort has been devoted by several laboratories to elucidate in more detail the arrangements between the subunits from the structural point of view to better understand the oxygenation of this giant hemoglobin. The three most important contributions in this research are associated with the mass spectrometry determination of the molecular masses of all subunits (3), to the three-dimensional reconstructions at a low resolution of 35 Å obtained by cryoelectron microscopy (1) and which were able to give results o...

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“…Studies on the interactions between surfactants and proteins would be beneficial for understanding the occurence of surfactants acting as solubilizing or denaturing agents for proteins [7,8]. For example, serum albumins are the most abundant proteins in blood plasma and are the major soluble protein in the circulatory system [9].…”

Section: Introductionmentioning

confidence: 99%

Fluorescence Spectroscopy Study on the Interaction of Acetal Cleavable Anionic Surfactants and Bovine Serum Albumin

et al. 2014

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The interactions between bovine serum albumin (BSA) and two cleavable anionic surfactants, sodium 3-[(2-nonyl-1,3-dioxolan-4-yl)methoxy]propane-1-sulfonate (SNPS) and sodium 3,3 -(2-nonyl-1,3-dioxane-5,5-diyl)bis(methylene)bis(oxy)dipropane-1-sulfonate (SNDPS), have been studied by means of fluorescence spectroscopy and thermodynamic analysis. The fluorescence of BSA is quenched via a static quenching mechanism with the addition of the surfactants. The binding constants of the surfactants and proteins have been measured, with (SNPS) = 8.71 × 10 4 M −1 and (SNDPS) = 7.08 × 10 4 M −1 , respectively. The interaction between surfactants and BSA is mainly of hydrophobic nature, based on the number of binding sites, n[n(SNPS) = 1.57, n(SNDPS) = 1.47], and the thermodynamic relationship. These results suggest that SNPS and SNDPS could be effective protein denaturants for protein separation and analysis.

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Surfactant interactions with biomembranes and proteins

Cited by 357 publications

References 23 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

Small Angle X-ray Scattering (SAXS) Study of the Extracellular Hemoglobin of Glossoscolex paulistus

Fluorescence Spectroscopy Study on the Interaction of Acetal Cleavable Anionic Surfactants and Bovine Serum Albumin

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