A light scattering study of interactions of oppositely charged proteins in solution

ABSTRACTIn experiments involving electrophoresis of proteins in gels, it was observed that the mobility of FITC tagged albumin (FITC albumin) was greater than that of TRITC tagged albumin (TRITC albumin). To further understand the effects of tagging proteins with fluorescent dyes, interactions of anionic proteins FITC albumin and untagged bovine serum albumin (BSA), with cationic protein ploy-L-lysine was studied using dynamical light scattering. It was found that aggregates formed by the interaction of FITC albumin with poly-L-lysine were larger than those formed by the interaction between poly-L-lysine and BSA. Using zeta potential measurements it was observed that irrespective of the fluorescent tags attached to them, the zeta potential values of cationic proteins changed from negative to positive with increasing amounts of poly-L-lysine. It was also observed that addition of small amounts of poly-L-lysine to solutions containing FITC albumin decreased the zeta potential drastically. To explain this data, we are proposing a model that suggests that low concentrations of poly-L-lysine serve as scaffold - like structures on which several FITC albumin molecules anchor. We conclude that FITC appears to change the surface charge of albumin significantly and thereby influencing its behavior in solution and its interaction with cationic poly-L-lysine.