Protein unfolding by SDS: the microscopic mechanisms and the properties of the SDS-protein assembly

Winogradoff, David; John, Shalini; Aksimentiev, Aleksei

doi:10.1039/c9nr09135a

Cited by 42 publications

(37 citation statements)

References 106 publications

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“…Therefore, the sequential formation of micelle-like structures occurs, and a decorated micelle structure is formed. Although the formation of pearl-necklace structures has been previously reported for ionic surfactants and proteins, 3,43 no evidence of these structures, within the concentration range investigated here, has been found. It is hypothesised that the driving mechanism for the pearl-necklace structure is similar to that of the decorated micelle model, where the hydrophobic residues of the micelle are preferably adsorbed at the micelle core and the hydrophilic groups remain in contact with the solvent.…”

Section: Papercontrasting

confidence: 50%

An integrative toolbox to unlock the structure and dynamics of protein–surfactant complexes

et al. 2020

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Section: Papercontrasting

confidence: 50%

An integrative toolbox to unlock the structure and dynamics of protein–surfactant complexes

et al. 2020

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“…It is well known that SDS dissolves proteins due to the disruption of secondary bonds. [ 20 ] The high solubility of the unaged PNF foams indicates that these foams contained very few covalent crosslinks. The aging treatment polymerized the protein creating new covalent bonds, which stabilized the foams.…”

Section: Resultsmentioning

confidence: 99%

High‐Temperature and Chemically Resistant Foams from Sustainable Nanostructured Protein

Capezza

Gowda

et al. 2021

Advanced Sustainable Systems

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Covalently crosslinked protein networks produced from whey protein nanofibrils (PNFs) are demonstrated to be sustainable high‐performance foams that show chemical resistance and mechanical strength, stiffness, and toughness on harsh aging at 150 °C. The aged foams are able to retain their properties at 180 °C for as long as 24 h, far exceeding the properties of most classical petroleum‐based thermoplastics. The foams are further developed into soft foams by the addition of glycerol as a plasticizer. The improvement in the mechanical performance of the foams with aging, which is equivalent to an increase by one order of magnitude in modulus and yield strength, is confirmed to be associated with (iso)peptide crosslinks. The results open the way for using protein‐based foam materials in severe/corrosive environments such as filtration, thermal insulation, and fluid absorption. The protein foams produced are suggested as suitable alternatives to petroleum‐based porous polymers.

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“…The effect of further addition of high concentration of SDS after they completely unfolded, was the micellization around the protein backbone. The interaction between anionic head of SDS to the cationic group of BSA still remain while the SDS molecules were forming micelle [20]. Those SDS micelles formed bead-like along the BSA chain.…”

Section: Resultsmentioning

confidence: 97%

“…In this study, the SANS scattering data of BSA in addition of SDS below CMC fitted with the triaxial ellipsoid model, a simple shape approach for protein globular structure. It is previously reported that the initial interaction of SDS and protein is the binding of SDS molecule to the loop and the b-sheet part [20]. The addition of 2mM SDS led to invasion of SDS molecule to the loop of BSA and it seemed that the further addition of 5mM SDS still happened in the loop part as BSA do not have b-sheet content.…”

Section: Resultsmentioning

confidence: 98%

Sans Studies on the Bovine Serum Albumin Denaturation in the Presence of SDS

Rahayu

Patriati

Suparno

et al. 2021

jsmi

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The effect of the presence of sodium dodecyl sulfate (SDS) on the denaturation of bovine serum albumin (BSA) has been studied using 36 m small-angle neutron scattering (SANS) BATAN spectrometer (SMARTer). The neutron scattering data reduction used the Graphical Reduction and Analysis SANS Program (GRASP) software, and the fitting process used the IGOR SANS Analysis software. The denaturation process was identified by observing the changes BSA globular structure. The experimental results showed the addition of SDS at low concentrations (2 mM, 5 mM, 10 mM) into BSA solution at pH 7 do not cause a significant change in the size of the BSA globular structure. The SANS scattering profile of BSA fitted with the triaxial ellipsoid model, a simple shape approach for protein globular structure. The fitting result showed the semi-axis B for BSA in the addition of 2 mM, 5 mM, 10 mM SDS were 33.8 Å, 33.8 Å, and 37.8 Å, respectively. While the semi-axis A and semi-axis C were constant for those three variations at 14.6 Å and 32.2 Å, respectively. In higher addition of SDS, the globular structure of BSA unfolded into flexible cylinder structure with the radius of 14.4 Å and length of 83.5 Å. The denaturation of BSA was clearly showed by the addition of 40 mM SDS. The structure of BSA in this condition fitted to fractal structure with fractal dimension of 1.1, the block radius of 16.7 Å and the correlation length of 42.5 Å. These results indicated that the addition of SDS at low concentrations has not caused the denaturation of BSA. Meanwhile, the addition of SDS at high concentrations made BSA to unfold that lead to the denaturation of BSA.

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Protein unfolding by SDS: the microscopic mechanisms and the properties of the SDS-protein assembly

Abstract: Molecular dynamics simulations reveal how anionic surfactant SDS and heat unfold full-length proteins.

Cited by 42 publications

References 106 publications

An integrative toolbox to unlock the structure and dynamics of protein–surfactant complexes

An integrative toolbox to unlock the structure and dynamics of protein–surfactant complexes

High‐Temperature and Chemically Resistant Foams from Sustainable Nanostructured Protein

Sans Studies on the Bovine Serum Albumin Denaturation in the Presence of SDS

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