Chemical stabilized nanomaterials have enjoyed success as multifunctional therapeutic, diagnostic, catalytic properties and resolved a number of issues associated on interaction with biological systems. But they are unable to conquer the pricey synthetic route and production of chemical hazards. To triumph over this inadequacy, a one-step economically benign cost-effective synthesis of silver nanoparticles from a renewable plant, S. asper, was proclaimed and its infliction on photocatalytic efficiency, antibacterial activity and interaction with human serum albumin (HSA) was described. The characterization of nanoparticles was well esteemed by UV-vis, DLS, HR-TEM, FE-SEM, XRD, FT-IR and zeta potential assessment. The degree of crystallinity and size of the synthesized nanoparticles obtained from HR-TEM (similar to 13 nm) was convincingly commensurate the XRD data. The nanoparticles effectively fascinate the degradation of toxic phenothiazinium dye methylene blue and anthropogenic contaminant 4-nitrophenol in a short course time. The nanoparticles were revealed good antibacterial activity against Escherichia coli ATCC 25922. Due to limited understanding of protein-nanoparticles associated outcome, the study on the interaction of nanoparticles is very decisive on investigating interactions with specific biological systems. Thus, in order to explicit the protein-nanoparticles binding utility to a high resolution, herein we demonstrate the interaction study of HSA with S. asper stabilized silver nanoparticles (SNPs).Absorption, fluorescence spectroscopic studies exhibit the existence of similar to 10(8) orders binding upon interaction. Thermodynamic parameter (Delta G) indicated that the process was spontaneous. The fluorescence lifetime measurement revealed the subsistence of static binding mechanism, evolves via ground state HSA-SNPs binary complex formation. CD spectral study explored upon interaction protein structure was unaltered with slight decrement in alpha-helix content (56.2% to 52.9%). High negative zeta potential of HSA-SNPs (-49.4 mV) complex compared to SNPs (-253 mV) substantiated the stabilization of HSA-SNPs complex with the formation of protein on the nanoparticles surface. (C) 2018 Elsevier B.V. All rights reserved.
