RESUMEN
The binding between two surface-active substituted 3H-indole fluorescence probes, i. e., iodo-dihexadecyl methyl-2-(p-dodecyl amino phenyl)-3, 3-dimethyl-5-carboethoxy-3H-indole ammonium and iodo-dimethyloctadecyl-2-(p-dodecyl amino phenyl)-3,3-dimethyl-5-carboethoxy-3H-indole ammonium, and bovine serum albumin (BSA) in aqueous solution was studied using fluorescence. The binding constant and binding site number of molecule 1 and molecule 2 with BSA were obtained. It was confirmed that electrostatic interaction is the primary driving force for the combination of BSA with molecule 1 or molecule 2. According to the Förster resonance energy transfer theory, the distances between molecule 1, molecule 2 and tryptophan of BSA were calculated to be 2.90 nm and 4.02 nm, respectively.
Asunto(s)
Colorantes Fluorescentes/química , Albúmina Sérica Bovina/química , Algoritmos , Animales , Bovinos , Colorantes Fluorescentes/metabolismo , Indoles/química , Indoles/metabolismo , Cinética , Estructura Molecular , Unión Proteica , Albúmina Sérica Bovina/metabolismo , Espectrometría de Fluorescencia , Electricidad EstáticaRESUMEN
A substituted 3H-indole quaternary ammonium molecule was designed and synthesized using hexamethylphosphoramide (HMPA) as a solvent. The products were purified and characterized by IR, 1H-NMR, MS and elemental analysis. The binding reaction of this compound with bovine serum albumin (BSA) in aqueous solution was studied using fluorescence. Their binding constant is Ka = 1.995 x 10(5) dm3 x mol(-1) and the binding site number is n = 1.12. It is confirmed that the combination is a single static quenching process.