Presentation Title

Modelling the Chemical Repair of Protein Carbon-Centered Radicals with Glutathione

Format of Presentation

Poster to be presented Friday March 31, 2017

Abstract

Glutathione (GSH) is a tripeptide of non-protein origin that contains cysteine, glycine, and glutamate, which the human body can synthesize. It is an important antioxidant found in the highest concentration in the liver. It has been suggested that the thiol (-SH) group of GSH can help repair free radicals formed through hydrogen-transfer reactions. In this work, the thermodynamics and the kinetics of the chemical repair of radical-damaged leucine residues by GSH in hydrophilic and hydrophobic environments are studied using density functional theory.

Calculations are performed at the M06-2X-SMD/6-31++G(d,p) level of theory using N–formyl–leucinamide as a protein model. The radical-repair reactions studied are H-transfer reactions from the –SH site in GSH to each of the four carbon-centered radicals that can be formed from previous attacks to the lateral chain of the protein model used. This protein model was recently used to study the antioxidant capacity of dihydrolipoic acid (DHLA) following a similar repair mechanism.1 The results obtained in this work allow the antioxidant activity comparison between GSH and DHLA.

1 R. Castañeda-Arriaga, N. Mora-Diez, J. R. Alvarez-Idaboy, RCS Adv., 2015, 5, 96714-96719.

Department

Chemistry

Faculty Advisor

Nelaine Mora-Diez

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Modelling the Chemical Repair of Protein Carbon-Centered Radicals with Glutathione

Glutathione (GSH) is a tripeptide of non-protein origin that contains cysteine, glycine, and glutamate, which the human body can synthesize. It is an important antioxidant found in the highest concentration in the liver. It has been suggested that the thiol (-SH) group of GSH can help repair free radicals formed through hydrogen-transfer reactions. In this work, the thermodynamics and the kinetics of the chemical repair of radical-damaged leucine residues by GSH in hydrophilic and hydrophobic environments are studied using density functional theory.

Calculations are performed at the M06-2X-SMD/6-31++G(d,p) level of theory using N–formyl–leucinamide as a protein model. The radical-repair reactions studied are H-transfer reactions from the –SH site in GSH to each of the four carbon-centered radicals that can be formed from previous attacks to the lateral chain of the protein model used. This protein model was recently used to study the antioxidant capacity of dihydrolipoic acid (DHLA) following a similar repair mechanism.1 The results obtained in this work allow the antioxidant activity comparison between GSH and DHLA.

1 R. Castañeda-Arriaga, N. Mora-Diez, J. R. Alvarez-Idaboy, RCS Adv., 2015, 5, 96714-96719.