Octameric alcohol oxidase dissociates into stable, soluble monomers upon incubation with dimethylsulfoxide

Visser, Nina V.; Wang, Dongyuan; Stanley, Will A.; Groves, Matthew R.; Wilmanns, Matthias; Veenhuis, Marten; Klei, Ida J. van der

doi:10.1016/j.abb.2007.01.005

Cited by 8 publications

(4 citation statements)

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“…18 The few reports on the destabilizing effects of diluted DMSO mostly pertain to dissociation of oligomeric proteins. 19,20 On the other hand, at high concentrations, DMSO usually causes denaturation of proteins. 6,9,16 Apart from perturbing water−water and water− protein interactions, 21 one of the key mechanisms through which DMSO induces denaturation relies on its strong H-bond acceptor properties.…”

Section: ■ Introductionmentioning

confidence: 99%

“…Low concentrations of DMSO in water were shown to accelerate refolding of the denatured lysozyme and increase the enzymatic activity of glyceraldehyde-3-phosphate dehydrogenase . The few reports on the destabilizing effects of diluted DMSO mostly pertain to dissociation of oligomeric proteins. , On the other hand, at high concentrations, DMSO usually causes denaturation of proteins. ,, Apart from perturbing water–water and water–protein interactions, one of the key mechanisms through which DMSO induces denaturation relies on its strong H-bond acceptor properties. Protein conformation in DMSO can be accessed using infrared (IR) spectroscopy.…”

Section: Introductionmentioning

confidence: 99%

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β₂-Type Amyloidlike Fibrils of Poly-l-glutamic Acid Convert into Long, Highly Ordered Helices upon Dissolution in Dimethyl Sulfoxide

et al. 2018

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Replacing water with dimethyl sulfoxide (DMSO) completely reshapes the free-energy landscapes of solvated proteins. In DMSO, a powerful hydrogen-bond (HB) acceptor, formation of HBs between backbone NH groups and solvent is favored over HBs involving protein's carbonyl groups. This entails a profound structural disruption of globular proteins and proteinaceous aggregates (e.g., amyloid fibrils) upon transfer to DMSO. Here, we investigate an unusual DMSO-induced conformational transition of β 2amyloid fibrils from poly-L-glutamic acid (PLGA). The infrared spectra of β 2 -PLGA dissolved in DMSO lack the typical features associated with disordered conformation that are observed when amyloid fibrils from other proteins are dispersed in DMSO. Instead, the frequency and unusual narrowness of the amide I band imply the presence of highly ordered helical structures, which is supported by complementary methods, including vibrational circular dichroism and Raman optical activity. We argue that the conformation most consistent with the spectroscopic data is that of a PLGA chain essentially lacking nonhelical segments such as bends that would provide DMSO acceptors with direct access to the backbone. A structural study of DMSO-dissolved β 2 -PLGA by synchrotron small-angle X-ray scattering reveals the presence of long uninterrupted helices lending direct support to this hypothesis. Our study highlights the dramatic effects that solvation may have on conformational transitions of large polypeptide assemblies.

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Section: ■ Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

β₂-Type Amyloidlike Fibrils of Poly-l-glutamic Acid Convert into Long, Highly Ordered Helices upon Dissolution in Dimethyl Sulfoxide

et al. 2018

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“…Likewise, low concentrations of DMSO in water have been found to increase the rate of refolding of denatured lysozyme . Destabilizing effects of diluted DMSO are usually confined to dissociation of oligomeric proteins (e.g., refs and ). At higher concentrations, by contrast, DMSO increasingly reveals a denaturating influence on proteins. ,, The dependence of a protein’s conformational stability on the fractional volume of DMSO is complex, which in part follows from the strongly nonideal behavior of the water/DMSO system. − DMSO not only perturbs the “microstructure” of water, but since it is a strong H-bond acceptor and a good solvent for apolar side groups, DMSO can also affect a protein through direct binding to its surface.…”

Section: Introductionmentioning

confidence: 99%

On the DMSO-Dissolved State of Insulin: A Vibrational Spectroscopic Study of Structural Disorder

et al. 2012

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Upon dissolving in dimethyl sulfoxide (DMSO), native insulin and insulin amyloid fibrils convert into an identical disordered structural state based on IR spectral characteristics. Here, we investigate the DMSO-denatured state of insulin using a number of spectroscopic methods: near-UV circular dichroism, infrared absorption spectroscopy, vibrational circular dichroism (VCD), Raman scattering, and Raman optical activity (ROA), as well as by carrying out 140-ns-long molecular dynamics (MD) simulations of DMSO-dissolved native insulin monomers. According to this work, the DMSO-solvated state of insulin is an ensemble of conformations including polyproline II-type helix and possibly a residual α-helical structure. Effects of DMSO-specific solvation and conformation-restricting covalent structure of insulin (including the three intact disulfide bridges) are argued to play important roles in stabilizing the disordered state of the protein. A comparison of ROA spectra of insulin dissolved in fully deuterated and nondeuterated DMSO suggested transfer of chirality from the protein to the otherwise ROA-silent solvent. Our study provides an example of a biological protein that acquires a substantial population of PP II conformation in an entirely nonaqueous environment. The DMSO-unfolded state of insulin and its dynamics are also discussed in the context of the established link between PP II conformation and protein misfolding.

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“…The AOx (alcohol: oxygen oxidoreductases, EC 1.1.3.13) from Pichia pastoris is a massive protein with molecular weight of ~600 KDa, each subunits consisting of a noncovalently bound flavin adenine dinucleotide as a cofactor [13]. The subunit molecular mass of AOx has been reported as ~75 KDa and association of the subunits attributed to the hydrophobic interactions [14].…”

Section: Introductionmentioning

confidence: 99%

Microwave based reversible unfolding and refolding of alcohol oxidase protein probed by fluorescence and circular dichroism spectroscopy

Chinnadayyala¹,

Santhosh²,

Goswami³

2012

JBPC

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The reversible effect of microwave mediated denaturation of protein at low exposure time of 10 s has been demonstrated for the first time. The effect of microwave (2.45 GHz and 900 W) was confirmed in a homo-octameric alcohol oxidase in aqueous solution of pH 7.5. The unfolding events did not transverse through any intermediate states and no subunits of the protein were detached during the process. The refolding of the protein achieved at 4˚C for 24 h had regenerated the native enzyme. This reversible refolding approach excludes any chemical reagent and therefore established as simple technique for protein unfolding-folding studies.

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Octameric alcohol oxidase dissociates into stable, soluble monomers upon incubation with dimethylsulfoxide

Cited by 8 publications

References 20 publications

β₂-Type Amyloidlike Fibrils of Poly-l-glutamic Acid Convert into Long, Highly Ordered Helices upon Dissolution in Dimethyl Sulfoxide

β₂-Type Amyloidlike Fibrils of Poly-l-glutamic Acid Convert into Long, Highly Ordered Helices upon Dissolution in Dimethyl Sulfoxide

On the DMSO-Dissolved State of Insulin: A Vibrational Spectroscopic Study of Structural Disorder

Microwave based reversible unfolding and refolding of alcohol oxidase protein probed by fluorescence and circular dichroism spectroscopy

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Octameric alcohol oxidase dissociates into stable, soluble monomers upon incubation with dimethylsulfoxide

Cited by 8 publications

References 20 publications

β2-Type Amyloidlike Fibrils of Poly-l-glutamic Acid Convert into Long, Highly Ordered Helices upon Dissolution in Dimethyl Sulfoxide

β2-Type Amyloidlike Fibrils of Poly-l-glutamic Acid Convert into Long, Highly Ordered Helices upon Dissolution in Dimethyl Sulfoxide

On the DMSO-Dissolved State of Insulin: A Vibrational Spectroscopic Study of Structural Disorder

Microwave based reversible unfolding and refolding of alcohol oxidase protein probed by fluorescence and circular dichroism spectroscopy

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Product

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β₂-Type Amyloidlike Fibrils of Poly-l-glutamic Acid Convert into Long, Highly Ordered Helices upon Dissolution in Dimethyl Sulfoxide

β₂-Type Amyloidlike Fibrils of Poly-l-glutamic Acid Convert into Long, Highly Ordered Helices upon Dissolution in Dimethyl Sulfoxide