Adsorptive voltammetric investigation of the interaction of cisplatin with cystine and human serum albumin.

The interaction of the anti-cancer drug cisplatin with human serum albumin and cystine has been investigated using differential pulse adsorptive voltammetry. Based on an understanding of the voltammetric behaviour of these biological molecules, which rely on the presence of the disulphide groups within their molecular structure for their electroactivity, it has been postulated that binding of cisplatin to these molecules occurs at the disulphide bond. A fractional coefficient for the binding of cisplatin to human serum albumin at pH 7.4 was calculated to be 0.32. The reactivity of hydrolysis products of cisplatin was shown to be greater than that of the parent drug.