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Nitric oxide-releasing alpha-tocopherol mimetics with LDL-protective activity were designed to maintain the tocopherol substructure necessary for its biochemical recognition by alpha-tocopherol transfer protein. In order to study the molecular interactions to alpha-TTP, theoretical binding studies by means of docking techniques and experimental binding assays, using a fluorescent probe, were performed. Furoxanyl-tocopherol-hybrid analogs 7 and 9 have the best ability to bind to alpha-TTP suggesting that they could be incorporated to LDL in vivo to further release nitric oxide and prevent oxidative modifications.
Protein Conformation, Molecular Sequence Data, alpha-Tocopherol, Tocopherols, Cholesterol, LDL, Nitric Oxide, Antioxidants, Structure-Activity Relationship, Amino Acid Substitution, Humans, Vitamin E, Nitric Oxide Donors, Protein Binding
Protein Conformation, Molecular Sequence Data, alpha-Tocopherol, Tocopherols, Cholesterol, LDL, Nitric Oxide, Antioxidants, Structure-Activity Relationship, Amino Acid Substitution, Humans, Vitamin E, Nitric Oxide Donors, Protein Binding
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