Spectroscopic and Computational Analysis of Protein Binding on Copper Nanoparticles: an Insight into Ligand and Nanocarrier Interaction
| Autor: | D. Mallaiah, G. Chakravarthy, M. Ramanadham, S. A. A. Latheef |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
Circular dichroism
Quenching (fluorescence) 010304 chemical physics biology Chemistry Cooperative binding Langmuir adsorption model 02 engineering and technology 021001 nanoscience & nanotechnology Condensed Matter Physics 01 natural sciences Binding constant Fluorescence spectroscopy Hydrophobic effect Crystallography symbols.namesake 0103 physical sciences biology.protein symbols Bovine serum albumin 0210 nano-technology Spectroscopy |
| Zdroj: | Journal of Applied Spectroscopy. 83:896-902 |
| ISSN: | 1573-8647 0021-9037 |
| DOI: | 10.1007/s10812-016-0381-3 |
| Popis: | The interaction of copper nanoparticles (CuNP) with bovine serum albumin (BSA) under physiological conditions was studied using spectroscopic techniques. The analysis of the adsorption of BSA by CuNP indicated that it followed the Langmuir adsorption isotherm and a pseudo second-order expression. The quenching of BSA intrinsic fluorescence was observed upon its binding to CuNP. The calculation of a modified Stern–Volmer constant revealed that the binding of CuNP to BSA complies with the static mechanism. The binding constant, the binding site, and the thermodynamic parameters of the BSA–CuNP interaction were evaluated using fluorescence quenching data at 298, 310, and 333 K. The binding constant decreased with increase in temperature, and the binding of BSA to CuNP involved one single site. Negative free energy (ΔG), positive enthalpy (ΔH), and entropy change (ΔS) calculations suggested that the binding of BSA to CuNP was spontaneous and hydrophobic forces played a key role in stabilizing the complex. An evaluation of the Hill coefficient indicated negative cooperativity. Minor conformational changes were observed in the circular dichroism spectra when BSA was bound to CuNP. |
| Databáze: | OpenAIRE |
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