http://www.cnr.it/ontology/cnr/individuo/prodotto/ID278661
Molecular interactions of hemoglobin with resveratrol: potential protective antioxidant role and metabolic adaptations of the erythrocyte (Articolo in rivista)
- Type
- Label
- Molecular interactions of hemoglobin with resveratrol: potential protective antioxidant role and metabolic adaptations of the erythrocyte (Articolo in rivista) (literal)
- Anno
- 2014-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1515/hsz-2013-0257 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Ester Tellone; Maria Cristina De Rosa; Davide Pirolli; Annamaria Russo; Bruno Giardina; Antonio Galtieri; Silvana Ficarra (literal)
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- Rivista
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- Department of Chemical Sciences, University of Messina, V. le Ferdinando Stagno d'Alcontres 31, I-98166 Messina, Italy
C.N.R. Institute of Chemistry of Molecular Recognition, L. go F. Vito n.1, I-00168 Rome, Italy
Biochemistry and Clinical Biochemistry Institute, Catholic University, School of Medicine, L. go F. Vito n.1, I-00168 Rome, Italy (literal)
- Titolo
- Molecular interactions of hemoglobin with resveratrol: potential protective antioxidant role and metabolic adaptations of the erythrocyte (literal)
- Abstract
- This article 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, the redox state, and 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 in the intracellular
concentration of ATP and with the decrease in ATP release from red blood cell and the consequent paracrine
alteration on the vascular epithelium. Molecular docking calculations indicate larger specificity of binding for oxyhemoglobin
that correlates well 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 the 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. (literal)
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