Open Science Research Excellence
%0 Journal Article
%A S. Ashrafpour and  T. Tohidi Moghadam and  B. Ranjbar
%D 2014 
%J  International Journal of Chemical and Molecular Engineering
%B World Academy of Science, Engineering and Technology
%I International Science Index 93, 2014
%T Fluorescence Spectroscopy of Lysozyme-Silver Nanoparticles Complex
%U http://waset.org/publications/9999348
%V 93
%X Identifying the nature of protein-nanoparticle
interactions and favored binding sites is an important issue in
functional characterization of biomolecules and their physiological
responses. Herein, interaction of silver nanoparticles with lysozyme
as a model protein has been monitored via fluorescence spectroscopy.
Formation of complex between the biomolecule and silver
nanoparticles (AgNPs) induced a steady state reduction in the
fluorescence intensity of protein at different concentrations of
nanoparticles. Tryptophan fluorescence quenching spectra suggested
that silver nanoparticles act as a foreign quencher, approaching the
protein via this residue. Analysis of the Stern-Volmer plot showed
quenching constant of 3.73 μM−1. Moreover, a single binding site in
lysozyme is suggested to play role during interaction with AgNPs,
having low affinity of binding compared to gold nanoparticles.
Unfolding studies of lysozyme showed that complex of lysozyme-
AgNPs has not undergone structural perturbations compared to the
bare protein. Results of this effort will pave the way for utilization of
sensitive spectroscopic techniques for rational design of
nanobiomaterials in biomedical applications.

%P 985 - 988