Monitoring the interactions between bovine serum albumin and ZnO/Ag nanoparticles by spectroscopic techniques

Inducing the bio-functionalization in noble metal nanoparticles like gold, silver, zinc is very important to accomplish their biocompatibility in biological activities. These metal nanoparticles are being rigorously used in bio-sensing tools keeping their remarkable properties in mind. Amongst the serum albumins, the most ample proteins in plasma are bovine serum albumin and human serum albumin. A broad variety of physiological functions of bovine serum albumin has made it a model protein for bio-functionalization. In the present study, ZnO/Ag nanoparticles were synthesized and characterized by SEM and XRD techniques and the interaction between bovine serum albumin and ZnO/Ag nanoparticles was evaluated by employing ultra-violet, steady state fluorescence, circular dichroism and FTIR spectroscopic techniques. Upon the excitation of bovine serum albumin, ZnO/Ag nanoparticles appreciably reduced the intrinsic fluorescence intensity of bovine serum albumin. The number of binding locations and apparent binding constants at different temperatures were calculated by the fluorescence quenching method. Static mechanism of quenching and conformational modifications in bovine serum albumin were also found. Communicated by Ramaswamy H. Sarma

Automated summary

Inducing bio-functionalization in noble metal nanoparticles is crucial for their biocompatibility in biological activities. In this study, ZnO/Ag nanoparticles were synthesized and their interaction with bovine serum albumin was evaluated. The results showed that ZnO/Ag nanoparticles significantly reduced the intrinsic fluorescence intensity of bovine serum albumin and induced conformational modifications.