access icon free Probing the in vitro binding mechanism between human serum albumin and La2O2CO3 nanoparticles

© The Institution of Engineering and Technology
Received 03/08/2017, Accepted 20/11/2017, Revised 19/10/2017, Published 23/11/2017

The interaction of La2O2CO3 nanoparticles (La NPs) with human serum albumin (HSA) has been studied. Analysis of the fluorescence quenching data of HSA using Stern–Volmer method showed that La NPs quenched HSA fluorescence in static quenching mode. Thermodynamic analysis indicated that hydrogen bonds and Van der Waals interactions play a major role for HSA–La NPs associations. Fluorescent displacement measurements confirmed that the primary binding site of La NPs was mainly located within site I (subdomain IIA) of HSA. The binding distance was calculated by using Forster resonance energy transfer theory. Also, the results of Fourier-transform infrared spectroscopy, circular dichroism, three-dimensional fluorescence and UV–visible measurements indicated that the binding of above La NPs to HSA may induce conformational and micro-environmental changes of protein. This study suggested that the conformational change of HSA was at secondary structure of it and the biological activity of this protein was changed in the present of La NPs.

Inspec keywords: hydrogen bonds; molecular configurations; Fourier transform infrared spectra; fluorescence; biothermics; lanthanum compounds; visible spectra; nanoparticles; ultraviolet spectra; van der Waals forces; molecular biophysics; thermal analysis; proteins; nanobiotechnology; radiation quenching; biochemistry; circular dichroism

Other keywords: La2O2CO3 nanoparticles; secondary structure; in vitro binding mechanism; static quenching mode; fluorescent displacement measurements; La2O2CO3; three-dimensional fluorescence; Fourier-transform infrared spectroscopy; protein; circular dichroism; human serum albumin; thermodynamic analysis; UV-visible measurements; Forster resonance energy transfer theory; La NPs quenched HSA fluorescence; Stern-Volmer method; microenvironmental changes; binding distance; Van der Waals interactions; conformational changes; hydrogen bonds; primary binding site; HSA-La NPs associations; subdomain IIA

Subjects: Structure of solid clusters, nanoparticles, nanotubes and nanostructured materials; Electronic structure and spectra of macromolecules; Interactions with radiations at the biomolecular level; Molecular bond strengths, dissociation energies, hydrogen bonding; Physical chemistry of biomolecular solutions and condensed states; Molecular fluorescence and phosphorescence spectra; Ultraviolet molecular spectra; Intramolecular energy transfer; intramolecular dynamics; dynamics of van der Waals molecules; Biothermics; Biomolecular interactions, charge transfer complexes; Crystal binding; Optical activity, optical rotation, circular dichroism in molecules; Biomolecular structure, configuration, conformation, and active sites; Other methods of nanofabrication; Infrared molecular spectra; Magneto-optical and electro-optical effects in atoms; birefringence, dichroism and optical activity; Visible molecular spectra; Macromolecular configuration (bonds, dimensions)

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