Interaction studies between human α-tocopherol transfer protein and nitric oxide donor tocopherol analogues with LDL-protective activity

Nitric oxide-releasing α-tocopherol mimetics with LDL-protective activity were designed to maintain the tocopherol substructure necessary for its biochemical recognition by α-tocopherol transfer protein. In order to study the molecular interactions to α-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 α-TTP suggesting that they could be incorporated to LDL in vivo to further release nitric oxide and prevent oxidative modifications.

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