Study on the interaction between oxolinic acid aggregates and protein and its analytical application.

It was found that oxolinic acid (OA) at high concentration can self-assemble into nano- to micro-meter scale OA aggregates in Tris-HCl (pH 7.48) buffer solution. The nanoparticles of OA were adopted as fluorescence probes in the quantitative analysis of proteins. Under optimum conditions, the fluorescence quenching extent of nanometer scale OA aggregates was in proportion to the concentration of albumins in the range of 3.0x10(-8) to 3.0x10(-5) g mL(-1) for bovine serum albumin (BSA) and 8.0x10(-8) to 8.0x10(-6) g mL(-1) for human serum albumin (HSA). The detection limits (S/N=3) were 3.4x10(-9) g mL(-1) for BSA, and 2.6x10(-8) g mL(-1) for HSA, respectively. Samples were satisfactorily determined. The interaction mechanism of the system was studied using fluorescence, UV-vis, resonance light scattering (RLS) and transmission electron microscope (TEM) technology, etc., indicating that the nonluminescent complex was formed between serum albumin molecular and OA, to disaggregate the self-association of OA, which resulted in the dominated static fluorescence quenching in the system.