Copyright © 2026 Authors retain the copyright of this article. This article is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
@article{191268,
author = {S.N.Chougale and Dr. V.R. More and Dr. A.D.Chougale and Prof. G.B. Kolekar and Prof. P. Dandage and S. K. Kumbhar and S.V. Koparde and P.D. Sanadi},
title = {Fluorescence Spectroscopic Analysis of Silver Nanoparticles Interaction with Bovine Serum Albumin and its Biological Implications.},
journal = {International Journal of Innovative Research in Technology},
year = {2026},
volume = {12},
number = {8},
pages = {7455-7463},
issn = {2349-6002},
url = {https://ijirt.org/article?manuscript=191268},
abstract = {Nanoparticles (NPs) come into contact with protein-containing fluids, such as biological fluids, and they quickly accumulate a layer of proteins on their surface, known as the protein corona. The composition and structure of this protein corona are crucial for determining how the nanoparticles interact with living cells. The interaction between silver nanoparticles (AgNPs) and bovine serum albumin (BSA) was examined using various methods, including fluorescence quenching, dynamic light scattering (DLS), and zeta potential analysis. The adsorption resulted in a significant gradual increase in the average hydrodynamic radius of the AgNPs protein corona from 30nm to 40nm. Changes in the zeta potential charge on the surface of AgNPs, and the AgNPs protein corona led to an increase in stability in the AgNPs protein corona compared to AgNPs (-18 to -30 (mV). Functional groups of AgNPs were changed by protein functional groups, as revealed by FT-IR analysis. Scanning Electron Microscopy (SEM) and Energy Dispersive X-ray (EDX) studies confirmed the spherical nature of the synthesised particles, as observed by TEM. Fluorescence quenching data of BSA by AgNPs protein corona showed the formation of a 1:1 ground state complex using the Stern–Volmer method. Evaluation of binding parameters and binding energy indicated that the binding reaction was exothermic. In the study of cell cytotoxicity, BSA-AgNPs exhibited greater cytotoxicity than unmodified AgNPs due to the formation of a protein corona, enhancing their suitability for biological applications.},
keywords = {Ag Nanoparticles, chemical method, protein interaction, Bovine serum Albumin, Protein corona},
month = {January},
}
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