Probing the in vitro binding mechanism between human serum albumin and La ₂ O ₂ CO ₃ nanoparticles

Abstract

The interaction of La 2 O 2 CO 3 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 microenvironmental 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.

Improvement of efficacy and decrement cytotoxicity of oxaliplatin anticancer drug using bovine serum albumin nanoparticles: synthesis, characterisation and release behaviour

“…To date, protein-based nanocarriers due to the non-toxic, non-immunogenic, biodegradable and biocompatible, frequency of its source, its cheap price, its easy separation and purification was used for DDS [4]. Specifically, albumin nanoparticles due to stability in blood circulation, its high ability for ligand binding and its acceptability in the pharmaceutical industry are a suitable candidate for nanocarriers of anticancer drugs [4][5][6]. Presence of high amounts of albumin in the body causes injection of significant amounts of it to the body without complications or with low side effects.…”