Investigation of the interaction of alkyl sulphates with serum albumin using the thiocyanate radical ion (SCN)2.
The reaction of the radical anion -(SCN)2-, produced during pulse radilysis of aqueous KCNS solutions, have been used to study the binding of a range of alkyl sulphates to bovine (BSA) and human (HSA) serum albumin. At neutral pH, -(SCN)2- reacts chiefly with trytophan residues. Approximately ten high-affinity binding sites are detectable for compounds of chain length greater than C7. The results are interpreted in terms of a model in which one hydrophobic region in the protein, containing the tryptophan residues, can accommodate the ten ligand molecules. Electrostatic interactions with positively-charged groups surrounding the hydrophobic area are also involved in binding.
D006801:Humans; D066298:In Vitro Techniques; D011485:Protein Binding; D011675:Pulse Radiolysis; D012709:Serum Albumin; D012710:Serum Albumin, Bovine; D013464:Sulfuric Acids; D013861:Thiocyanates
D012709:Serum Albumin; D013464:Sulfuric Acids; D013861:Thiocyanates; D012710:Serum Albumin, Bovine