This paper reports the role of resveratrol in the erythrocyte as a result of its interaction with hemoglobin, and describes the effect of this interaction on the metabolism, on the redox state and on the release of ATP. The drug crosses the erythrocyte membrane and binds to hemoglobin altering its modulation and the release of ATP. Our study, correlates the variation of the phosphorylation balance induced by resveratrol, with the change of the intracellular concentration of ATP, with the decrease of ATP release from red blood cell and the consequent paracrine alteration on the vascular epithelium. Molecular docking calculations indicate larger specificity of binding for oxy-hemoglobin that well correlates with the stabilization of the R-quaternary structure and with the functional modulation of resveratrol on the protein. Finally, we locate a putative binding site at central cavity of hemoglobin and characterize its key interacting residues with the drug. Computational results support the assumption that resveratrol may act as a protector agent against oxidative protein damage by interacting with hemoglobin.
Molecular interactions of hemoglobin with resveratrol: potential protective antioxidant role and metabolic adaptations of the erythrocyte
TELLONE, Ester;RUSSO, Annamaria;GALTIERI, Antonio;FICARRA, Silvana
2014-01-01
Abstract
This paper reports the role of resveratrol in the erythrocyte as a result of its interaction with hemoglobin, and describes the effect of this interaction on the metabolism, on the redox state and on the release of ATP. The drug crosses the erythrocyte membrane and binds to hemoglobin altering its modulation and the release of ATP. Our study, correlates the variation of the phosphorylation balance induced by resveratrol, with the change of the intracellular concentration of ATP, with the decrease of ATP release from red blood cell and the consequent paracrine alteration on the vascular epithelium. Molecular docking calculations indicate larger specificity of binding for oxy-hemoglobin that well correlates with the stabilization of the R-quaternary structure and with the functional modulation of resveratrol on the protein. Finally, we locate a putative binding site at central cavity of hemoglobin and characterize its key interacting residues with the drug. Computational results support the assumption that resveratrol may act as a protector agent against oxidative protein damage by interacting with hemoglobin.Pubblicazioni consigliate
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