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The Effect of a Hydrogen Bonding Environment (Dimethyl Sulfoxide) on the Ionisation and Redox Properties of the Thiol Group in Cysteine and a Protein Disulfide Isomerase Mimic (Vectrase)
Authors:Jaanus Kruusma  Aidan Rhodes  Radhika Bhatia  J. A. Gareth Williams  Adam M. Benham  Ritu Kataky
Affiliation:(1) Department of Chemistry, The Centre for Bioactive Chemistry, University of Durham, South Road, Durham, DH1 4HT, U.K.;(2) Department of Biological and Biomedical Sciences, University of Durham, South Road, Durham, DH1 4HT, U.K.
Abstract:Increasing enrichment of dimethyl sulfoxide, DMSO, in DMSO-water mixtures causes a reversal in the thermodynamic dissociation constants, pK as, and has a marked effect on the redox potentails of the thiolic and amino groups in cysteine and the protein disulfide isomerase (PDI) mimic BMC, Vectrase. This paper illustrates the effect of a hydrogen-bonding environment on the ionisation and redox properties of thiol groups in amino acids. A combination of potentiometry and Raman spectroscopy was applied to rationalise the observations. Intracellular environments are full of hydrophobic, hydrogen-bonding environments. The results illustrate the profound effects of the local environment on the thiol group.
Keywords:Thiol  Dissociation constant  Redox properties  Hydrogen bonding  DMSO  Aqueous
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