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• W4312062402 startingPage "44" @default.
• W4312062402 abstract "Protein-ligand-exchange kinetics determines the duration of biochemical signals and consequently plays an important role in drug design. Binding studies commonly require solubilization of designed ligands in solvents such as dimethyl sulfoxide (DMSO), resulting in residual amounts of DMSO following titration of solubilized ligands into aqueous protein samples. Therefore, it is critical to establish whether DMSO influences protein-ligand binding. Here, we address the general and indirect effect of DMSO on protein-ligand binding caused by solvent viscosity, which is strongly dependent on the relative concentrations of DMSO and water. As a model system, we studied the binding of a drug-like ligand to the carbohydrate recognition domain of galectin-3 in the presence of variable amounts of DMSO. We used isothermal titration calorimetry to characterize binding thermodynamics and 15N NMR relaxation to monitor kinetics. The binding enthalpy is not affected, but we observe a subtle trend of increasingly unfavorable entropy of binding, and consequently decreased affinity, with increasing DMSO concentration. The increasing concentration of DMSO results in a reduced association rate of binding, while the dissociation rate is less affected. The observed association rate is inversely proportional to the viscosity of the DMSO-water mixture, as expected from theory, but significantly reduced from the diffusion-controlled limit. By comparing the viscosity dependence of the observed association rate with that of the theoretical diffusion-controlled association rate, we estimate the success rate of productive complex formation following an initial encounter of proteins and ligands, showing that only one out of several hundred binding attempts are successful." @default.
• W4312062402 created "2023-01-04" @default.
• W4312062402 creator A5014991622 @default.
• W4312062402 creator A5063659458 @default.
• W4312062402 creator A5072198977 @default.
• W4312062402 date "2022-12-21" @default.
• W4312062402 modified "2023-10-14" @default.
• W4312062402 title "Cosolvent Dimethyl Sulfoxide Influences Protein–Ligand Binding Kinetics via Solvent Viscosity Effects: Revealing the Success Rate of Complex Formation Following Diffusive Protein–Ligand Encounter" @default.
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• W4312062402 doi "https://doi.org/10.1021/acs.biochem.2c00507" @default.
• W4312062402 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36542811" @default.
• W4312062402 hasPublicationYear "2022" @default.
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