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Influence of bovine serum albumin on corrosion behaviour of pure Zn in phosphate buffered saline.

ABSTRACT: Zinc (Zn) and its alloys have received increasing attention as new alternative biodegradable metals. However, consensus has not been reached on the corrosion behaviour of Zn. As cardiovascular artery stent material, Zn is supposed to contact with plasma that contains inorganic salts and organic components. Protein is one of the most important constitute in the plasma and could adsorb on the material surface. In this paper, bovine serum albumin (BSA) was used as a typical protein. Influences of BSA on pure Zn corrosion in phosphate buffered saline is investigated as a function of BSA concentrations and immersion durations by electrochemical techniques and surface analysis. Results showed that pure Zn corrosion was progressively accelerated with BSA concentrations (ranging from 0.05 to 5 g L^-1) at 0.5 h. With time evolves, formation of phosphates as corrosion product was delayed by BSA adsorption, especially at concentration of 2 g L^-1. Within 48 h, the corrosion of pure Zn was alleviated by BSA at concentration of 0.1 g L^-1, whereas the corrosion was enhanced after 168 h. Addition of 2 g L^-1 BSA has opposite influence on the pure Zn corrosion. Furthermore, schematic corrosion behaviour at protein/Zn interfaces was proposed. This work encourages us to think more about the influence of protein on the material corrosion and helps us to better understand the corrosion behaviour of pure Zn.

SUBMITTER: Liu L

PROVIDER: S-EPMC8373726 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Preservation Method and Phosphate Buffered Saline Washing Affect the Acute Myeloid Leukemia Proteome.

Project description:Acute myeloid leukemia (AML) primary cells can be isolated from peripheral blood, suspended with media containing bovine serum and cryoprotectant, and stored in liquid nitrogen before being processed for proteomic analysis by mass spectrometry (MS). The presence of bovine serum and human blood proteins in AML samples can hamper the identifications of proteins, and thereby reduce the proteome coverage of the study. Herein, we have established the effect of phosphate buffered saline (PBS) washing on AML patient samples stored in media. Although PBS washes effectively removed serum and blood contaminants, the saline wash resulted in cell burst and remarkable protein material loss. We also compared different methods to preserve the AML proteome from THP-1 and Molm-13 cell lines before MS analysis: (1) stored in media containing bovine serum and dimethyl sulfoxide (DMSO); (2) stored as dried cell pellets; and (3) stored as cell lysates in 4% sodium dodecyl sulfate (SDS). MS analysis of differently preserved AML cell samples shows that preservation with DMSO produce a high number of fragile cells that will burst during freezing and thawing. Our studies encourage the use of alternative preservation methods for future MS analysis of the AML proteome.

| S-EPMC5796241 | biostudies-literature

Denaturation studies on bovine serum albumin-bile salt system: Bile salt stabilizes bovine serum albumin through hydrophobicity.

Project description:Protein denaturation is under intensive research, since it leads to neurological disorders of severe consequences. Avoiding denaturation and stabilizing the proteins in their native state is of great importance, especially when proteins are used as drug molecules or vaccines. It is preferred to add pharmaceutical excipients in protein formulations to avoid denaturation and thereby stabilize them. The present study aimed at using bile salts (BSs), a group of well-known drug delivery systems, for stabilization of proteins. Bovine serum albumin (BSA) was taken as the model protein, whose association with two BSs, namely sodium cholate (NaC) and sodium deoxycholate (NaDC), was studied. Denaturation studies on the pre-formed BSA-BS systems were carried out under chemical and physical denaturation conditions. Urea was used as the chemical denaturant and BSA-BS systems were subjected to various temperature conditions to understand the thermal (physical) denaturation. With the denaturation conditions prescribed here, the data obtained is informative on the association of BSA-BS systems to be hydrophobic and this effect of hydrophobicity plays an important role in stabilizing the serum albumin in its native state under both chemical and thermal denaturation.

| S-EPMC5859114 | biostudies-literature

Expression data from Staphylococcus aureus and Phosphate buffered saline (PBS) treated mouse wound bed

Project description:Environmental factors that enhance regeneration are largely unknown. We hypothesized that skin bacteria modulate regeneration. Here, we assessed low, medium, and high levels of bacterial burden in Wound Induced Hair follicle Neogenesis (WIHN), a rare adult organogenesis model. WIHN levels and stem cell markers indeed correlated with bacterial counts, being lowest in germ free (GF), intermediate in conventional specific pathogen free (SPF), and highest even in mice infected with pathogenic Staphylococcus aureus. We identified IL-1β and keratinocyte-dependent IL-1R-MyD88 signaling as necessary and sufficient for bacteria to promote regeneration. Finally, in a small clinical trial, we found that a topical broad-spectrum antibiotic slowed skin wound healing. These results counter conventional notions that infection inhibits regeneration and the need for full sterility of small wounds.

2021-04-01 | GSE158614 | GEO

The novel behaviour of interactions between Ni2+ ion and human or bovine serum albumin.

Project description:We discovered a series of novel behaviours of interactions between Ni2+ ion and human or bovine serum albumin. Our results indicated that there exist two closely neighbouring identical prior binding sites in the binding of human or bovine serum albumin with Ni2+ ions, not only one. It is very likely that, after the binding of the first Ni2+ ion, an induced slow conformational transition happens, which leads to the binding of the second Ni2+ ion and shows itself as a hysteretic effect for a process of non-enzymic protein binding with metal ions. As the concentrations of the 1:1 (molar ratio of Ni2+ ion to protein) system increase, an increasing hypochromic effect is observed. Such a hypochromic effect has not been reported previously; however, it is in accord with the mechanism of dipole-dipole interactions between the electric dipole transition moments of chromophores.

| S-EPMC1137445 | biostudies-other

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

Project description: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.

| S-EPMC7077681 | biostudies-literature

Proteolysis of Iron Oxide-Associated Bovine Serum Albumin.

Project description:Proteins are a substantial nitrogen source in soils provided that they can be hydrolyzed into bioavailable small peptides or amino acids. However, the strong associations between proteins and soil minerals restrict such proteolytic reactions. This study focused on how an extracellular fungal protease (Rhizopus sp.) hydrolyzed iron oxide-associated bovine serum albumin (BSA) and the factors that affected the proteolysis. We combined batch experiments with size-exclusion and reversed phase liquid chromatography and in situ infrared spectroscopic measurements to monitor the generation of proteolytic products in solution as well as the real-time changes of the adsorbed BSA during 24 h. Results showed that protease hydrolyzed the iron oxide-associated BSA directly at the surface without an initial desorption of BSA. Concurrently, the protease was adsorbed to vacant surface sites at the iron oxides, which significantly slowed down the rate of proteolysis. This inhibiting effect was counteracted by the presence of preadsorbed phosphate or by increasing the BSA coverage, which prevented protease adsorption. Fast initial rates of iron oxide-associated BSA proteolysis, comparable to proteolysis of BSA in solution, and very slow rates at prolonged proteolysis suggest a large variability in mineral-associated proteins as a nitrogen source in soils and that only a fraction of the protein is bioavailable.

| S-EPMC7311061 | biostudies-literature

Biogenic and synthetic polyamines bind bovine serum albumin.

Project description:Biogenic polyamines are found to modulate protein synthesis at different levels, while polyamine analogues have shown major antitumor activity in multiple experimental models, including breast cancer. The aim of this study was to examine the interaction of bovine serum albumin (BSA) with biogenic polyamines, spermine and spermidine, and polyamine analogues 3,7,11,15-tetrazaheptadecane x 4 HCl (BE-333) and 3,7,11,15,19-pentazahenicosane x 5 HCl (BE-3333) in aqueous solution at physiological conditions. FTIR, UV-visible, CD, and fluorescence spectroscopic methods were used to determine the polyamine binding mode and the effects of polyamine complexation on protein stability and secondary structure. Structural analysis showed that polyamines bind BSA via both hydrophilic and hydrophobic interactions. Stronger polyamine-protein complexes formed with biogenic than synthetic polyamines with overall binding constants of K(spm) = 3.56 (+/-0.5) x 10(5) M(-1), K(spmd) = 1.77 (+/-0.4) x 10(5) M(-1), K(BE-333) = 1.11 (+/-0.3) x 10(4) M(-1) and K(BE-3333) = 3.90 (+/-0.7) x 10(4) M(-1) that correlate with their positively charged amino group contents. Major alterations of protein conformation were observed with reduction of alpha-helix from 63% (free protein) to 55-33% and increase of turn 12% (free protein) to 28-16% and random coil from 6% (free protein) to 24-17% in the polyamine-BSA complexes, indicating a partial protein unfolding. These data suggest that serum albumins might act as polyamine carrier proteins in delivering polyamine analogues to target tissues.

| S-EPMC2886673 | biostudies-literature

Corrosion Behavior and In Vitro Cytotoxicity of Ni-Ti and Stainless Steel Arch Wires Exposed to Lysozyme, Ovalbumin, and Bovine Serum Albumin.

Project description:In this study, the tendency and mechanisms by which protein and mechanical loads contribute to corrosion were determined by exposing Ni-Ti and stainless steel arch wires under varying mechanical loads to artificial saliva containing different types of protein (lysozyme, ovalbumin, and bovine serum albumin). The corrosion behavior and in vitro cytotoxicity results show that exposure to both protein and mechanical stress significantly decreased the corrosion resistance of stainless steel and increased the release of toxic corrosion products. Adding protein inhibited the corrosion of Ni-Ti, but the mechanical loads counteracted this effect. Even proteins containing the same types of amino acids had different effects on the corrosion resistance of the same alloy. The effect of protein or stress, or their combination, should be considered in the application of metal medical materials.

| S-EPMC7408227 | biostudies-literature

Reversible pH Responsive Bovine Serum Albumin Hydrogel Sponge Nanolayer.

Project description:A pH dependent reversible sponge like behavior of a bovine serum albumin (BSA) nanolayer adsorbed at the gold-saline interface is revealed by quartz crystal microbalance with dissipation (QCM-D), atomic force microscope (AFM) and contact angle measurements. During the saline rinsing cycles, the BSA layer adsorbs water molecules at pH 7.0 and releases them at pH 4.5. The phenomenon remains constant and reproducible upon multiple rinsing cycles. The BSA layer thickness also increases upon rinsing with saline at pH 7.0 and reverses back to its original thickness at pH 4.5. Varying ionic strength with water further desorbs more water molecules from the BSA layer, which decreases its mass and thickness. However, upon both pH and ionic strength changes, all the BSA molecules remain adsorbed irreversibly at the gold interface and only the sorption of water molecules occurs. The study aims at engineering high efficiency pH-responsive biodiagnostics and drug delivery systems.

| S-EPMC7286146 | biostudies-literature

Purification and Characterization of Bovine Serum Albumin Using Chromatographic Method.

Project description:Purpose: Albumin is an abundant protein of blood and has many biopharmaceutical applications. The aim of this study was to purify bovine serum albumin (BSA) using produced rabbit anti-BSA antibody. Methods: The polyclonal antibody was produced against the BSA in rabbits. Then, the pure BSA was injected to three white New Zealand rabbits. ELISA test was done to evaluate antibody production. After antibody purification,the purified antibody was attached to CNBr-activated sepharose and finally it was used for purification of albumin from bovine serum. Western blotting analysis was used for functional assessment of immunoaffinity purified BSA. Results: The titer of anti-bovine albumin determined by ELISA was obtained 1: 256000. The SDS-PAGE showed up to 98% purity of isolated BSA and western blotting confirmed the BSA functionality. Purified bovine serum albumin by affinity chromatography showed a single band with molecular weight of 66 KDa. Conclusion: Affinity chromatography using produced rabbit anti-BSA antibody would be an economical and safe method for purification of BSA.

| S-EPMC5241424 | biostudies-literature

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