Monitoring the interactions between bovine serum albumin and ZnO/Ag nanoparticles by spectroscopic techniques
| Autor: | Umesha Katrahalli, Devagondanahalli H. Manjunatha, Basappa C. Yallur, Raju Kale, Abhishek Udnoor, Manjunath Lokolkar, Muttanagoud N. Kalasad |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
Circular dichroism
Silver Biocompatibility chemistry.chemical_element Nanoparticle Metal Nanoparticles Zinc engineering.material Structural Biology medicine Humans Bovine serum albumin Molecular Biology Quenching (fluorescence) Binding Sites biology Circular Dichroism Serum Albumin Bovine General Medicine Human serum albumin Spectrometry Fluorescence chemistry engineering biology.protein Thermodynamics Noble metal Zinc Oxide Nuclear chemistry medicine.drug Protein Binding |
| Zdroj: | Journal of biomolecular structuredynamics. 41(1) |
| ISSN: | 1538-0254 |
| Popis: | 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 |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|