Covalent Surface Functionalization of Bovine Serum Albumin to Magnesium Surface: Enhancing Robust Corrosion Inhibition and In vitro Osteo-Inductivity

Herein, we describe precisely on covalent modification of pure magnesium (Mg) surface and applied to induce in vitro osteogenic differentiation. A new concept, chemical bonding method is proposed for developing stable chemical bonds on Mg surface through serial assembly of bioactive additives including ascorbic acid (AA) and bovine serum albumin (BSA). The coating with such potential materials shows strong integrity to the Mg and could suitable for cell-interface interaction with the host tissue during implantation in bone tissue repair. The physicochemical and electrochemical properties of surface modified Mg assess how these nanoscales layered of biomolecules could demonstrate the significance improvement in chemical stability of coating. The modified Mg-OH-AA-BSA exhibits better anti-corrosion behavior with high corrosion potential (Ecorr ~ ‒ 0.96 V) and low corrosion current density (Icorr ~ 0.2 µA cm-2) as compared to pure Mg (Ecorr ~ ‒1.46 V, Icorr ~ 10.42 µA cm-2). Outer layer of BSA on Mg protects fast degradation rate of Mg which is the consequence of strong chemicals bonds between amine groups on BSA with carboxylic groups on AA. Collectively, the results suggest that surface modified Mg provides strong bio-interface and enhances the proliferation and differentiation of pre-osteoblast (MC3T3-E1) cells through protein-lipid interaction. Owing to this fact, the cost-effective and scalable covalent functionalization of Mg surface inherits biological advantage in orthopedic and dental implants with long term stability.

Download Full-text

Covalent Surface Functionalization of Bovine Serum Albumin to Magnesium Surface to Provide Robust Corrosion Inhibition and Enhance In Vitro Osteo-Inductivity

Polymers ◽

10.3390/polym12020439 ◽

2020 ◽

Vol 12 (2) ◽

pp. 439

Author(s):

Seo Yeon Lee ◽

Sita Shrestha ◽

Bishnu Kumar Shrestha ◽

Chan Hee Park ◽

Cheol Sang Kim

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Cost Effective ◽

Corrosion Current ◽

Covalent Modification ◽

Peptide Bonds ◽

Bonding Method ◽

Surface Modified

Herein, we describe precisely a covalent modification of pure magnesium (Mg) surface and its application to induce in vitro osteogenic differentiation. The new concept of a chemical bonding method is proposed for developing stable chemical bonds on the Mg surface through the serial assembly of bioactive additives that include ascorbic acid (AA) and bovine serum albumin (BSA). We studied both the physicochemical and electrochemical properties using scanning electron microscopy and other techniques to confirm how the covalent bonding of BSA on Mg can, after coating, significantly enhance the chemical stability of the substrate. The modified Mg-OH-AA-BSA exhibits better anti-corrosion behavior with high corrosion potential (Ecorr = −0.96 V) and low corrosion current density (Icorr = 0.2 µA cm−2) as compared to the pure Mg (Ecorr = −1.46 V, Icorr = 10.42 µA cm−2). The outer layer of BSA on Mg protects the fast degradation rate of Mg, which is the consequence of the strong chemicals bonds between amine groups on BSA with carboxylic groups on AA as the possible mechanism of peptide bonds. Collectively, the results suggest that the surface-modified Mg provides a strong bio-interface, and enhances the proliferation and differentiation of pre-osteoblast (MC3T3-E1) cells through a protein–lipid interaction. We therefore conclude that the technique we describe provides a cost-effective and scalable way to generate chemically stable Mg surface that inherits a biological advantage in orthopedic and dental implants in clinical applications.

Download Full-text

A Precipitin-like Reaction of the Hemolymph of the Lobster Homarus americanus

Journal of the Fisheries Research Board of Canada ◽

10.1139/f69-127 ◽

1969 ◽

Vol 26 (5) ◽

pp. 1392-1397 ◽

Cited By ~ 10

Author(s):

James E. Stewart ◽

Diane M. Foley

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Serum Proteins ◽

Homarus Americanus ◽

Test Period ◽

Fluorescent Material

The levels of fluorescent material in the hemolymph of lobsters injected with serum proteins from lobster hemolymph labelled with fluorescein remained relatively constant over a 6-day test period; the levels in lobsters injected with bovine serum albumin labelled with fluorescein declined rapidly. A precipitin-like reaction was observed when lobster hemolymph serum was titrated with bovine serum albumin in vitro.

Download Full-text

Preparation and in vitro photodynamic activities of novel axially substituted silicon (IV) phthalocyanines and their bovine serum albumin conjugates

Bioorganic & Medicinal Chemistry Letters ◽

10.1016/j.bmcl.2006.01.075 ◽

2006 ◽

Vol 16 (9) ◽

pp. 2450-2453 ◽

Cited By ~ 42

Author(s):

Xiong-Jie Jiang ◽

Jian-Dong Huang ◽

Yu-Jiao Zhu ◽

Fen-Xiang Tang ◽

Dennis K.P. Ng ◽

...

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum

Download Full-text

Amuchina Gel Xgerm hand rub in vitro virucidal activity against SARS-CoV-2

Future Microbiology ◽

10.2217/fmb-2021-0128 ◽

2021 ◽

Author(s):

Alessandra Capezzone de Joannon ◽

Angela Testa ◽

Natalie Falsetto ◽

Michela Procaccini ◽

Lorella Ragni

Keyword(s):

Detection Limit ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Virucidal Activity ◽

European Standard ◽

Enveloped Viruses ◽

Prevention Measure ◽

Study Product

Aim: Ethanol is highly effective at inactivating enveloped viruses, including SARS-CoV-2. The aim of this study is to evaluate the virucidal activity of Amuchina Gel Xgerm (74% ethanol) against SARS-CoV-2, according to the European Standard EN14476:2013+A2:2019. Materials & methods: Virucidal activity of the study product was evaluated against SARS-CoV-2 strain USAWA1/2020 in suspension, in the presence of 0.3 g/l of bovine serum albumin. Results: The log10 reduction of SARS-CoV-2 in the presence of bovine serum albumin was ≥4.11 ± 0.12 after 30 s of exposure to the study product (80% dilution). Cytotoxicity was observed in the 100 dilution, affecting the detection limit by 1 log10. Conclusion: Virucidal activity against SARS-CoV-2 supports the effectiveness of this alcohol-based formulation as a prevention measure for COVID-19 illness.

Download Full-text

In-vitro displacement interaction of atenolol and amlodipine on binding with bovine serum albumin when co-administered

Bangladesh Journal of Pharmacology ◽

10.3329/bjp.v2i1.496 ◽

2008 ◽

Vol 2 (1) ◽

Author(s):

Md Ashraful Alam ◽

Md Abdul Awal ◽

Mahbub Mostofa ◽

Md Kamrul Islam ◽

Nusrat Subhan

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum

Download Full-text

Bovine serum albumin (BSA) can replace patient serum as a protein source in an in vitro fertilization (IVF) program

Journal of In Vitro Fertilization and Embryo Transfer ◽

10.1007/bf01130782 ◽

1989 ◽

Vol 6 (3) ◽

pp. 164-167 ◽

Cited By ~ 8

Author(s):

Claudio A. Benadiva ◽

Barbara Kuczynski-Brown ◽

Tobi G. maguire ◽

Luigi Mastroianni ◽

George L. Flickinger

Keyword(s):

In Vitro Fertilization ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Protein Source ◽

Vitro Fertilization

Download Full-text

In Vitro Study of the Binding of Taxifolin to Bovine Serum Albumin and the Influence of Common Ions on the Binding

Journal of Solution Chemistry ◽

10.1007/s10953-010-9516-y ◽

2010 ◽

Vol 39 (4) ◽

pp. 482-494 ◽

Cited By ~ 9

Author(s):

Xiaolei Shi ◽

Xuwen Li ◽

Yantao Sun ◽

Wei Wei ◽

Ruijie Yang ◽

...

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

In Vitro Study ◽

Vitro Study

Download Full-text

Protein-polyelectrolyte complexes. Part 3. Complexes bovine serum albumin with sulfonate-containing aromatic poly- and copolyamides

Butlerov Communications ◽

10.37952/roi-jbc-01/19-58-4-66 ◽

2019 ◽

Vol 58 (4) ◽

pp. 66-71

Author(s):

Natalia N. Smirnova ◽

◽

Kirill V. Smirnov ◽

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Aromatic Polyamide ◽

Density Maximum ◽

Degree Of Ionization ◽

Polyelectrolyte Complexes ◽

Composition And Structure ◽

Carboxylic Groups ◽

Main Factor

The interaction of bovine serum albumin in aqueous solution with sulfonate-containing poly- and copolyamides were studied. It was shown that, as a result of macromolecular reactions protein-polyelectrolyte complexes forms, stabilized mainly by electrostatic forces. To characterize the protein-polyelectrolyte complexes composition the r parameter used, which is defines as the ratio of mass concentration of polyelectrolyte and protein. It was shown that the main factor determining the composition and structure of forming protein-polyelectrolyte complexes is the degree of ionization of functional groups, interacting in the polyelectrolyte reaction that is determined by the nature of those groups and the pH of the solution. The presen ce of sulfonate and carboxylic groups in the copolyamide composition gives an extra opportunity to regulate the protein-polyelectrolyte interactions. Using spectrophotometry were established that, in the studied system when the aromatic polyamide and bovine serum albumin are mixed at optimal pH conditions (рН < 4.9), complexes are formed, the composition of which corresponds to the value of r ~ 0.15 g/g. The degree of conversation in protein-polyelectrolyte reactions is close to 0.8. The size of the formed particles was about 2.2 μm. In the case of aromatic copolyamides that contain both sulfonate and carboxylic groups, an increase in concentration of carboxylic groups to 42 mol. % leads to a shift of the optical density maximum on the curve of turbidimetric titration in to the higher r values (~ 0.18 g/g) at pH = 3.5, when the carboxylic groups are non-ionized. The size of the formed complex particles was about ~ 150.0 nm, the fraction of micron-sized particles is about 5%. The degree of released protein is based on the conditions under which reaction take place and varies from 93 to 99%. The result obtained during this work can serve as a base for the effective methods of isolation and purifying of the target proteins development.

Download Full-text

Clearance and binding of native and defucosylated lactoferrin

Biochemical Journal ◽

10.1042/bj2120249 ◽

1983 ◽

Vol 212 (2) ◽

pp. 249-257 ◽

Cited By ~ 20

Author(s):

M J Imber ◽

S V Pizzo

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Specific Binding ◽

Gel Filtration ◽

Peritoneal Macrophages ◽

Mononuclear Phagocyte ◽

Stable Complex

These studies explore the role of carbohydrate recognition systems and the direct involvement of terminal alpha 1-3-linked fucose in the clearance of lactoferrin from the murine circulation and in the specific binding of lactoferrin to receptors on murine peritoneal macrophages. As previously reported, radiolabelled lactoferrin cleared very rapidly (t1/2 less than 1 min) after intravenous injection into mice. However, competing levels of ligands specific for the hepatic galactose receptor (asialo-orosomucoid), the hepatic fucose receptor (fucosyl-bovine serum albumin), and the mononuclear-phagocyte system pathway recognizing mannose, N-acetylglucosamine and fucose (mannosyl-, N-acetylglucosaminyl- and fucosyl-bovine serum albumin) did not block radiolabelled lactoferrin clearance in vivo or binding to mouse peritoneal macrophage monolayers in vitro. Almond emulsin alpha 1-3-fucosidase was used to prepare defucosylated lactoferrin in which 88% of the alpha 1-3-linked fucose was hydrolysed. No difference in clearance or receptor binding was observed between radiolabelled native and defucosylated lactoferrin. Fucoidin, a fucose-rich algal polysaccharide, completely inhibits the clearance in vivo and macrophage binding in vitro of lactoferrin. This effect, however, is probably not the result of competition for binding to the fucose receptor, since gel-filtration studies demonstrated formation of a stable complex between lactoferrin and fucoidin. The present results indicate that the lactoferrin-clearance pathway is distinct from several pathways mediating glycoprotein clearance through recognition of terminal galactose, fucose, N-acetylglucosamine or mannose. Furthermore, alpha 1-3-linked fucose on lactoferrin is not essential for lactoferrin clearance in vivo or specific binding to macrophage receptors in vitro.

Download Full-text