Open AccessProbing the in vitro binding mechanism between human serum albumin and La 2 O 2 CO 3 nanoparticles
Author(s) -
Shahraki Somaye,
Saeidifar Maryam,
Gomroki Masomeh
Publication year - 2018
Publication title -
iet nanobiotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.366
H-Index - 38
eISSN - 1751-875X
pISSN - 1751-8741
DOI - 10.1049/iet-nbt.2017.0190
Subject(s) - human serum albumin , circular dichroism , chemistry , fluorescence , quenching (fluorescence) , hydrogen bond , van der waals force , nanoparticle , förster resonance energy transfer , protein secondary structure , fluorescence spectroscopy , spectroscopy , fourier transform infrared spectroscopy , crystallography , analytical chemistry (journal) , materials science , molecule , nanotechnology , chromatography , organic chemistry , biochemistry , chemical engineering , physics , quantum mechanics , engineering
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 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.