scholarly journals Formation and Stabilization of Gold Nanoparticles in Bovine Serum Albumin Solution

Molecules ◽  
2019 ◽  
Vol 24 (18) ◽  
pp. 3395 ◽  
Author(s):  
Iulia Matei ◽  
Cristina Maria Buta ◽  
Ioana Maria Turcu ◽  
Daniela Culita ◽  
Cornel Munteanu ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Particle Growth ◽  
Protective Role ◽  
Amino Acid Residues ◽  
Buffer Solution ◽  
Paramagnetic Resonance ◽  
Tem Microscopy

The formation and growth of gold nanoparticles (AuNPs) were investigated in pH 7 buffer solution of bovine serum albumin (BSA) at room temperature. The processes were monitored by UV-Vis, circular dichroism, Raman and electron paramagnetic resonance (EPR) spectroscopies. TEM microscopy and dynamic light scattering (DLS) measurements were used to evidence changes in particle size during nanoparticle formation and growth. The formation of AuNPs at pH 7 in the absence of BSA was not observed, which proves that the albumin is involved in the first step of Au(III) reduction. Changes in the EPR spectral features of two spin probes, CAT16 and DIS3, with affinity for BSA and AuNPs, respectively, allowed us to monitor the particle growth and to demonstrate the protective role of BSA for AuNPs. The size of AuNPs formed in BSA solution increases slowly with time, resulting in nanoparticles of different morphologies, as revealed by TEM. Raman spectra of BSA indicate the interaction of albumin with AuNPs through sulfur-containing amino acid residues. This study shows that albumins act as both reducing agents and protective corona of AuNPs.

Bioceramic Hydroxyapatite Granules for Purification of Biotechnological Products

2011 ◽  
Vol 284-286 ◽  
pp. 1764-1769 ◽  
Author(s):  
Vitalijs Lakevics ◽  
Janis Locs ◽  
Dagnija Loca ◽  
Valentina Stepanova ◽  
Liga Berzina-Cimdina ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Phosphate Buffer ◽  
Bovine Serum ◽  
Phosphate Buffer Solution ◽  
Sorption Process ◽  
Buffer Solution ◽  
Ph Values ◽  
Bovine Serum Albumin Adsorption ◽  
Albumin Adsorption

Sorption experiments of bovine serum albumin (BSA) on hydroxyapatite (HAp) ceramic granules, prepared at three temperatures 900°C, 1000°C and 1150°C were performed at room temperature 18,6 °C and phosphate buffer, pH 5,83; 6.38 and 7,39. Thermal treatment contributed to the decrease of bovine serum albumin immobilization indicating that sorption process depended on HAp ceramics specific surface area and pH values of phosphate buffer solution. However, it was confirmed that granule size was also an important parameter for bovine serum albumin adsorption. As a result of these experiments, the most appropriate adsorption conditions and phosphate buffer pH values influence on to BSA sorption were analyzed.

A Highly Sensitive Glucose Biosensor Based on Gold Nanoparticles/Bovine Serum Albumin/Fe3O4 Biocomposite Nanoparticles

2016 ◽  
Vol 222 ◽  
pp. 1709-1715 ◽  
Author(s):  
Chuanxin He ◽  
Minsui Xie ◽  
Fei Hong ◽  
Xiaoyan Chai ◽  
Hongwei Mi ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Glucose Biosensor ◽  
Highly Sensitive

STUDY OF THE TRANSFORMATION OF NITROSYL IRON COMPLEX WITH N-ETHYLTHIOUREA LIGANDS IN MODEL BIOLOGICAL SYSTEMS

2021 ◽  
Author(s):  
Olesya Viktorovna Pokidova ◽  
◽  
Nina Sergeevna Emel’yanova ◽  
Alexander Vasilievich Kulikov ◽  
Alexander Ivanovich Kotelnikov ◽  
...  
Keyword(s):  
Amino Acid ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Reduced Glutathione ◽  
Decay Product ◽  
Iron Complex ◽  
Amino Acid Residues ◽  
Cationic Complex ◽  
Nitrosyl Iron Complex

The process of transformation of a mononuclear cationic complex with N-ethylthiourea ligands in Tris-HCl buffer, as well as in a reaction mixture with reduced glutathione and bovine serum albumin, has been studied. It was found that in the presence of glutathione, the complex dimer-izes, while its initial ligands are replaced by glutathione. In the presence of albumin, the decay product of the complex is coordinated with amino acid residues (Cys34 and His39) to form a protein-bound complex.

Bovine serum albumin/gold nanoparticles as a drug delivery system for Curcumin: experimental and computational studies

2019 ◽  
Vol 38 (15) ◽  
pp. 4644-4654 ◽  
Author(s):  
Bahareh Khodashenas ◽  
Mehdi Ardjmand ◽  
Mazyar Sharifzadeh Baei ◽  
Ali Shokuhi Rad ◽  
Azim Akbarzadeh Khiyavi
Keyword(s):  
Drug Delivery ◽  
Gold Nanoparticles ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Drug Delivery System ◽  
Delivery System ◽  
Bovine Serum ◽  
Computational Studies

scholarly journals Comparison of Gold Nanoparticles Deposition Methods and Their Influence on Electrochemical and Adsorption Properties of Titanium Dioxide Nanotubes

Materials ◽  
2020 ◽  
Vol 13 (19) ◽  
pp. 4269 ◽  
Author(s):  
Ewa Paradowska ◽  
Katarzyna Arkusz ◽  
Dorota G. Pijanowska
Keyword(s):  
Gold Nanoparticles ◽  
Titanium Dioxide ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Photoelectron Spectroscopy ◽  
Bovine Serum ◽  
Electrochemical Impedance ◽  
Electrochemical Characterizations ◽  
Titanium Dioxide Nanotubes ◽  
X Ray

The increasing interest of attachment of gold nanoparticles (AuNPs) on titanium dioxide nanotubes (TNTs) has been devoted to obtaining tremendous properties suitable for biosensor applications. Achieving precise control of the attachment and shape of AuNPs by methods described in the literature are far from satisfactory. This work shows the comparison of physical adsorption (PA), cyclic voltammetry (CV) and chronoamperometry (CA) methods and the parameters of these methods on TNTs properties. The structural, chemical, phase and electrochemical characterizations of TNTs, Au/TNTs, AuNPs/TNTs are carried out using scanning electron microscopy (SEM), electrochemical impedance spectroscopy, X-ray diffraction, X-ray photoelectron spectroscopy. The use of PA methods does not allow the deposition of AuNPs on TNTs. CV allows easily obtaining spherical nanoparticles, for which the diameter increases from 20.3 ± 2.9 nm to 182.3 ± 51.7 nm as a concentration of tetrachloroauric acid solution increase from 0.1 mM to 10 mM. Increasing the AuNPs deposition time in the CA method increases the amount of gold, but the AuNPs diameter does not change (35.0 ± 5 nm). Importantly, the CA method also causes the dissolution of the nanotubes layer from 1000 ± 10.0 nm to 823 ± 15.3 nm. Modification of titanium dioxide nanotubes with gold nanoparticles improved the electron transfer and increased the corrosion resistance, as well as promoted the protein adsorption. Importantly, after the deposition of bovine serum albumin, an almost 5.5-fold (324%) increase in real impedance, compared to TNTs (59%) was observed. We found that the Au nanoparticles—especially those with smaller diameter—promoted the stability of bovine serum albumin binding to the TNTs platform. It confirms that the modification of TNTs with gold nanoparticles allows the development of the best platform for biosensing applications.

Über Photoreaktionen und Lumineszenzverhalten von Eosin in wäßrigen Lösungen von β-Lactoglobulin, Rinderserumalbumin und Cystein

1966 ◽  
Vol 21 (4) ◽  
pp. 305-313 ◽  
Author(s):  
G. Reske ◽  
F. Nimmerfall ◽  
J. Stauff
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Amino Acid Residues ◽  
Group Activities ◽  
Photo Oxidation ◽  
Sh Groups ◽  
Spectral Changes ◽  
Sh Group ◽  
Β Lactoglobulin

Interactions of eosin with three different substrates, β-lactoglobuline, bovine serum albumin and cysteine, in aqueous solutions of pH 7 under illumination with light of wavelengths 5200—5400 Å are investigated by changes in absorption spectrum characteristics, SH-group activities and phosphorescence intensities.Only with bovine serum albumin the major part of protein conversion, as shown by spectral changes and diminution of SH-groups due to eosin-sensitized photo-oxidation. In β-lactoglobuline an oxidizing photoreaction occurs, by which eosin is vanishing to the same degree as the protein shows loss of SH-groups and spectral alterations indicating attack on aromatic amino acid residues. There is no red shift of the eosin absorption band at 5170 Å as is observed in solutions of bovine serum albumin, where the intensity of phosphorscence is about 100 fold compared with the intensity obtained by solutions of β-lactoglobulin.The aerobic eosin photoreaction in solutions of β-lactoglobulin is faster than aerobic photobleaching of the dye. Still faster is its bleaching photoreaction with cysteine, which is nearly independent of oxygen.

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