Study on the interaction of bovine serum albumin with acid cyanine 5R and its application in analysis

Abstract

A supramolecular complex of bovine serum albumin (BSA) with acid cyanine 5R (AC 5R, C.I. acid blue 113, C.I.: 26360) has been shown to form in Tris-HCl buffer solution (pH 7.42) by linear sweep voltammetry (LSV), fluorimetry, and spectrophotometry. The binding ratio and binding constant of BSA with AC 5R have been detected by LSV and fluorimetry. The binding mechanism is also preliminarily discussed. In Tris-HCl buffer solution (pH 7.42), AC 5R can easily be reduced on the mercury electrode, and it has a well-defined LSV peak current (Ip) and peak potential (Ep) at -0.65 V (vs. SCE). In the presence of BSA, the Ip of AC 5R decreases, and the peak potential (Ep) shifts to a more positive potential. The decrease of the second-order derivative of reductive peak current (deltaIp'') of AC 5R is proportional to the logarithm of BSA concentration in the range of 1.54 x 10(-8) mol x L(-1)-1.54 x 10(-5) mol x L(-1) (r = 0.9931-0.9977). The limit of detection of BSA is 9.0 x 10(-9) mol x L(-1). The relative standard deviation is 1.83% (n = 10), and the standard recovery is 97.5%-104.8%. This method can be used to determine BSA concentration on the basis of the interaction of BSA with AC 5R.