Surface chemistry of bovine serum albumin with hematite nanoparticles and its effect on arsenate adsorption

2021 ◽  
Vol 18 (4) ◽  
pp. 177
Author(s):  
A. M. Eid ◽  
Shea Kraemer ◽  
Hind A. Al-Abadleh
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Surface Chemistry ◽  
Adsorption Kinetics ◽  
Bovine Serum ◽  
Active Sites ◽  
Binding Free Energy ◽  
Biological Systems ◽  
Hematite Nanoparticles ◽  
Arsenate Adsorption

Environmental contextHematite nanoparticles are efficient adsorbents for proteins and pollutants in environmental and biological systems. Hematite and the protein bovine serum albumin (BSA) were used as models to investigate the surface chemistry and competitive role of BSA in arsenate adsorption. Results show that surface BSA inhibits arsenate adsorption, potentially altering its mobility and bioavailability. AbstractThe surface chemistry of metal oxide nanomaterials controls their health impacts and fate in environmental and biological systems. These systems contain proteins capable of binding to nanoparticles, which forms a protein corona that modifies the surface properties of the nanoparticles and reactivity towards pollutants. Using attenuated total reflectance-Fourier transform infrared (ATR-FTIR) spectroscopy, we investigate the adsorption of bovine serum albumin (BSA) and quantify the competitive effect of BSA on the adsorption kinetics of arsenate, AsV, to hematite nanoparticles. Experiments were conducted in the flow mode at pH 7. BSA was first adsorbed on hematite, then AsV was allowed to flow over the BSA/hematite thin film. Adsorption kinetic and thermodynamic parameters were calculated using a modified Langmuir adsorption model for both BSA and AsV. The adsorption thermodynamic model showed that BSA binds through two active sites with a binding energy of –41 kJ mol−1, which corresponds to the spontaneous formation of chemisorbed and physisorbed species. When AsV flowed over the BSA/hematite film, only 11 % of surface BSA was desorbed by AsV. This result highlights the inhibitory effect of BSA for AsV adsorption. Structural analysis of BSA revealed changes to the local conformational geometry upon adsorption to and desorption from hematite nanoparticles. Molecular docking simulations showed that the binding free energy of a modelled hematite nanoparticle towards the BSA surface is –6.8 kcal mol−1 (−28.5 kJ mol−1) owing to the formation of various bonds, which agrees with the adsorption kinetics modelling. Overall, surface BSA inhibits arsenate adsorption and therefore increases its mobility and bioavailability.

Emerging investigator series: protein adsorption and transformation on catalytic and food-grade TiO2 nanoparticles in the presence of dissolved organic carbon

2019 ◽  
Vol 6 (6) ◽  
pp. 1688-1703 ◽  
Author(s):  
Junyeol Kim ◽  
Kyle Doudrick
Keyword(s):  
Titanium Dioxide ◽  
Bovine Serum Albumin ◽  
Organic Carbon ◽  
Serum Albumin ◽  
Surface Chemistry ◽  
Protein Adsorption ◽  
Bovine Serum ◽  
Titanium Dioxide Nanoparticles ◽  
Food Grade ◽  
Exposure History

The adsorption and unfolding behavior of bovine serum albumin onto catalytic- and food-grade titanium dioxide nanoparticles is dependent on the surface chemistry of the nanoparticles and their environmental exposure history.

BSA Adsorption on Hydroxyapatite after Thermal Treatment

2007 ◽  
Vol 361-363 ◽  
pp. 127-130 ◽  
Author(s):  
Elena Mavropoulos ◽  
Nilce C.C. da Rocha ◽  
Maria Helena M. Rocha-Leão ◽  
Antonella M. Rossi
Keyword(s):  
Thermal Treatment ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Phosphate Buffer ◽  
Bovine Serum ◽  
Active Sites ◽  
Sorption Process ◽  
Buffer Concentration ◽  
Surface Active ◽  
Bsa Adsorption

Adsorption experiments of bovine serum albumin on hydroxyapatite previously annealed at temperatures up to 1100°C was performed at 37°C and phosphate buffer, pH 6.0. Kinetic process was very efficient and irreversible for low phosphate buffer concentration. Thermal treatment contributed to the decrease of bovine serum albumin immobilization indicating that sorption process depended on HA specific surface area and the number of surface active sites. However, it was verified that particle size was also an important parameter for bovine serum albumin immobilization.

Thermodynamics, Conformation and Active Sites of the Binding of Zn–Nd Hetero-bimetallic Schiff Base to Bovine Serum Albumin

2008 ◽  
Vol 19 (2) ◽  
pp. 317-326 ◽  
Author(s):  
Qi Xiao ◽  
Shan Huang ◽  
Yi Liu ◽  
Fang-fang Tian ◽  
Jun-cheng Zhu
Keyword(s):  
Schiff Base ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Active Sites

Surface properties of bovine serum albumin – adsorbed oxides: Adsorption, adsorption kinetics and electrokinetic properties

2006 ◽  
Vol 96 (1-3) ◽  
pp. 331-340 ◽  
Author(s):  
Mahir Alkan ◽  
Özkan Demirbaş ◽  
Mehmet Doğan ◽  
Oktay Arslan
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Surface Properties ◽  
Adsorption Kinetics ◽  
Bovine Serum ◽  
Electrokinetic Properties

scholarly journals Spectroscopic, voltammetry and molecular docking study of binding interaction of antipsychotic drug with bovine serum albumin

2016 ◽  
Vol 6 (2) ◽  
pp. 155 ◽  
Author(s):  
Mallappa Mahanthappa ◽  
Babu Giriya Gowda ◽  
Jayant I. Gowda ◽  
Raghavendran Rengaswamy
Keyword(s):  
Molecular Docking ◽  
Bovine Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Free Energy ◽  
Acetate Buffer ◽  
Acetate Buffer Solution ◽  
Binding Interaction ◽  
Vis Spectroscopy

<p class="PaperAbstract"><span lang="EN-GB">The interaction between perazine dimaleate (PDM) and bovine serum albumin (BSA) was investigated by voltammetry, fluorescence spectroscopy, UV–vis spectroscopy, molecular docking and viscometric methods. The study was carried out in acetate buffer solution of pH 7.2, which was prepared by using 0.1 M sodium acetate and adjusting pH using 0.1 M hydrochloric acid. The voltammetric study of PDM shows a pair of well redox peaks at 0.538 and 0.471 V (versus SCE) on a GCE in acetate buffer of pH 7.2 at <br /> 50 mV s<sup>-1</sup>. After the addition of BSA into the PDM solution, the redox peak currents decreased gradually, and peak potentials shifted towards negative direction. The results of voltammetry, fluorescence quenching and UV–vis absorption spectra experiments indicated the formation BSA–PDM complex. The binding parameters like binding con­stant and binding free energy were determined from voltammetric data. The binding constant and binding energy was also determined from UV–vis and fluorescence spectroscopy with a value quite close to that obtained from CV.</span></p>

Surface chemistry of gold nanoparticles determines interactions with bovine serum albumin

2019 ◽  
Vol 103 ◽  
pp. 109856 ◽  
Author(s):  
Gongke Wang ◽  
Changling Yan ◽  
Shuyan Gao ◽  
Yufang Liu
Keyword(s):  
Gold Nanoparticles ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Surface Chemistry ◽  
Bovine Serum

scholarly journals Extraction behaviors of aqueous PEG impregnated resin system in terms of impregnation stability and recovery via protein impregnated resin interactions on bovine serum albumin

PeerJ ◽  
2021 ◽  
Vol 9 ◽  
pp. e11920
Author(s):  
Nur Fazrin Husna Abdul Aziz ◽  
Sahar Abbasiliasi ◽  
Mazni Abu Zarin ◽  
Hui Suan Ng ◽  
Chiwei Lan ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Adsorption Kinetics ◽  
Salt Solution ◽  
Bovine Serum ◽  
Aqueous Salt Solution ◽  
Phase System ◽  
Target Product ◽  
Resin System ◽  
Impregnated Resin

Background Current advances in biotechnology have been looked at as alternative approaches towards the limited product recovery due to time- and cost-consuming drawbacks on the conventional purification methods. This study aimed to purify bovine serum albumin (BSA) as an exemplary target product using an aqueous impregnated resin system (AIRS). This method implies the concept of hydrophobicity of polymer that impregnated into the resins and driven by electrostatic attractions and hydrophilicity of aqueous salt solution to extract the target product. Methods The extraction behaviors of impregnation in terms of stability and adsorption kinetics via protein-aqueous polymer impregnated resin were studied. Impregnation stability was determined by the leaching factor of polyethylene glycol (PEG). The major factors such as PEG molecular weights and concentration, pH of aqueous salt solution, extraction methods (sonication and agitation) and types of adsorbent material and concentration of aqueous salt phase influencing on partitioning of biomolecule were also investigated. Results For impregnation stability, the leaching factor for Amberlite XAD4 did not exceed 1%. The scanning electron microscopy (SEM) image analysis of Amberlite XAD4 attributes the structural changes with impregnation of resins. For adsorption kinetics, Freundlich adsorption isotherm with the highest R2 value (0.95) gives an indication of favorable adsorption process. Performance of AIRS impregnated with 40% (w/w) of PEG 2000 was found better than aqueous-two phase system (ATPS) by yielding the highest recovery of BSA (53.72%). The outcomes of this study propound the scope for the application of AIRS in purification of biomolecules.

Molybdenum-95 n.m.r. spectroscopy as a probe of biological systems: the detection of tetraoxo- and tetrathio-molybdate(VI) bound to bovine serum albumin

1985 ◽  
pp. 479 ◽  
Author(s):  
Stuart Bristow ◽  
C. David Garner ◽  
Stuart K. Hagyard ◽  
Gareth A. Morris ◽  
John R. Nicholson ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Biological Systems
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