Immobilization of Bovine Serum Albumin on Titanium through Plasma Polymerization of Allylamine and Crylic Acid

2007 ◽  
Vol 361-363 ◽  
pp. 713-716
Author(s):  
H.Q. Rao ◽  
Jian Xin Wang ◽  
X. Lu ◽  
Bo Feng ◽  
Jie Weng
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Photoelectron Spectroscopy ◽  
Bovine Serum ◽  
Plasma Polymerization ◽  
Titanium Surface ◽  
X Ray ◽  
Infrared Reflection Absorption Spectroscopy ◽  
Infrared Reflection ◽  
Work Technique

In the present work, technique of plasma polymerization was used to generate amido (- NH2) and carboxyl (-COOH) on titanium surface for immobilizing bovine serum albumin (BSA). After plasma polymerization of allylamine and crylic acid, the contact angle with respect to double distilled water significantly increased. Surface components were detected by X-ray photoelectron spectroscopy and Fourier transform infrared reflection-absorption spectroscopy. The results showed that BSA was successfully immobilized on the titanium surface and the amounts of BSA on specimens were relied on the properties of thin film deposited through plasma polymerization, which was corresponding to the ultraviolet spectrophotometer result.

The Influence of Calcium at the Titanium Surface on Co-Precipitation of Ca-P and Bovine Serum Albumin

2005 ◽  
Vol 475-479 ◽  
pp. 2375-2378
Author(s):  
Bo Feng ◽  
Jie Weng ◽  
Shao Xing Qu ◽  
Xing Dong Zhang
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Photoelectron Spectroscopy ◽  
Bovine Serum ◽  
Titanium Surface ◽  
Carbonate Apatite ◽  
X Ray ◽  
Phosphate Ions ◽  
Titanium Surfaces ◽  
Co Precipitation

The influence of calcium (Ca) at titanium surface on co-precipitation of Ca-P and bovine serum albumin (BSA) has been investigated by scanning electron microscopy, X-ray photoelectron spectroscopy and X-ray diffraction. The titanium surface containing Ca was prepared by immersing titanium plates into a saturated calcium hydroxyl (Ca(OH)2) solution. A solution containing BSA, calcium and phosphate ions was used for the co-precipitation test. Both BSA and calcium phosphate co-precipitated onto titanium surfaces with and without Ca. For the former, however, a thicker carbonate apatite coating, which consisted of finer crystal grains, formed and more protein precipitated compared to the surface without Ca. These results indicated that Ca at the titanium surface was favorable to the co-precipitation of BSA and Ca-P. Moreover, chemical interactions probably occurred during the co-precipitation of BSA and Ca-P.

Interaction of Bovine Serum Albumin and Lysozyme with Stainless Steel Studied by Time-of-Flight Secondary Ion Mass Spectrometry and X-ray Photoelectron Spectroscopy

Langmuir ◽  
2012 ◽  
Vol 28 (47) ◽  
pp. 16306-16317 ◽  
Author(s):  
Yolanda S. Hedberg ◽  
Manuela S. Killian ◽  
Eva Blomberg ◽  
Sannakaisa Virtanen ◽  
Patrik Schmuki ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Stainless Steel ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Photoelectron Spectroscopy ◽  
Bovine Serum ◽  
Secondary Ion Mass Spectrometry ◽  
Time Of Flight ◽  
X Ray ◽  
Secondary Ion

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.

scholarly journals Bovine Serum Albumin-Immobilized Black Phosphorus-Based γ-Fe2O3 Nanocomposites: A Promising Biocompatible Nanoplatform

Biomedicines ◽  
2021 ◽  
Vol 9 (8) ◽  
pp. 858
Author(s):  
Atanu Naskar ◽  
Sohee Lee ◽  
Dongjoon Ko ◽  
Semi Kim ◽  
Kwang-sun Kim
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Photoelectron Spectroscopy ◽  
Bovine Serum ◽  
Biomedical Applications ◽  
Physical Interaction ◽  
High Sequence Identity ◽  
X Ray ◽  
Interactive Behavior

The interactions between proteins and nanoparticles need to be fully characterized as the immobilization of proteins onto various nanoplatforms in the physiological system often results in the change of surface of the protein molecules to avoid any detrimental issues related to their biomedical applications. Hence, in this article, the successful low-temperature synthesis of a BP-based γ-Fe2O3 (IB) nanocomposite and its interactive behavior with bovine serum albumin (BSA)—a molecule with chemical similarity and high sequence identity to human serum albumin—are described. To confirm the formation of γ-Fe2O3 and the IB nanocomposite, X-ray diffraction, transmission electron microscopy, and X-ray photoelectron spectroscopy analyses of the materials were performed. Additionally, the physical interaction between BSA and the IB nanocomposite was confirmed via UV–Vis and photoluminescence spectral analyses. Finally, the biocompatibility of the BSA-immobilized IB nanocomposite was verified using an in vitro cytotoxicity assay with HCT-15 colon cancer cells. Our findings demonstrate that this newly developed nanocomposite has potential utility as a biocompatible nanoplatform for various biomedical applications.

scholarly journals Novel Bovine Serum Albumin Protein Backbone Reassembly Study: Strongly Twisted β-Sheet Structure Promotion upon Interaction with GO-PAMAM

Polymers ◽  
2020 ◽  
Vol 12 (11) ◽  
pp. 2603
Author(s):  
Andra Mihaela Onaș ◽  
Iuliana Elena Bîru ◽  
Sorina Alexandra Gârea ◽  
Horia Iovu
Keyword(s):  
Secondary Structure ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Infrared Spectrometry ◽  
X Ray Diffraction ◽  
Protein Backbone ◽  
Raman Spectrometry ◽  
X Ray ◽  
Β Sheet

This study investigates the formation of a graphene oxide-polyamidoamine dendrimer complex (GO-PAMAM) and its association and interaction with bovine serum albumin (BSA). Fourier-transform infrared spectrometry and X-ray photoelectron spectrometry indicated the formation of covalent linkage between the GO surface and PAMAM with 7.22% nitrogen content in the GO-PAMAM sample, and various interactions between BSA and GO-PAMAM, including π-π* interactions at 291.5 eV for the binding energy value. Thermogravimetric analysis highlighted the increasing thermal stability throughout the modification process, from 151 to 192 °C for the 10% weight loss temperature. Raman spectrometry and X-ray diffraction analysis were used in order to examine the complexes’ assembly, showing a prominent (0 0 2) lattice in GO-PAMAM. Dynamic light scattering tests proved the formation of stable graphenic and graphenic-protein aggregates. The secondary structure rearrangement of BSA after interaction with GO-PAMAM was investigated using circular dichroism spectroscopy. We have observed a shift from 10.9% β-sheet composition in native BSA to 64.9% β-sheet composition after the interaction with GO-PAMAM. This interaction promoted the rearrangement of the protein backbone, leading to strongly twisted β-sheet secondary structure architecture.

Small-Angle X-Ray Scattering on Solutions of Carboxymethylcellulose and Bovine Serum Albumin

2005 ◽  
Vol 5 (4) ◽  
pp. 331-336 ◽  
Author(s):  
Sabrina M. Pancera ◽  
Rosangela Itri ◽  
Denise F. S. Petri
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Small Angle ◽  
Bovine Serum ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering
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