Bovine Serum Albumin Preparations Research Articles

Utilization of ultrasound and glycation to improve functional properties and encapsulated efficiency of proteins in anthocyanins.

The purpose of this study is to explore the optimal conditions for the preparation of bovine serum albumin (BSA)/casein (CA)-dextran (DEX) conjugates by ultrasonic pretreatment combined with glycation (U-G treatment). When BSA and CA were treated with ultrasound (40% amplitude, 10min), the grafting degree increased 10.57% and 6.05%, respectively. Structural analysis revealed that ultrasonic pretreatment changed the secondary structure, further affected functional properties of proteins. After U-G treatment, the solubility and thermal stability of BSA and CA was significantly increased, and the foaming and emulsifying capacity of proteins were also changed. Moreover, ultrasonic pretreatment and glycation exhibited a greater impact on BSA characterized with highly helical structure. Complexes fabricated by U-G-BSA/CA and carboxymethyl cellulose (CMC) exhibited protection on anthocyanins (ACNs), delaying the thermal degradation of ACNs. In conclusion, the protein conjugates treated by ultrasonic pretreatment combined with glycation have excellent functionality and are potential carrier materials.

Albumin-Based Nanoparticles for the Delivery of Doxorubicin in Breast Cancer.

Simple SummaryDoxorubicin (Dox) is a chemotherapeutic agent usually employed for the treatment of breast cancer. However, its use is limited because of the toxicities associated, and hence a proper delivery vehicle is necessary. In this sense, albumin-based nanocarriers are in the limelight for the successful delivery of chemotherapeutics because of safety, biocompatibility, and specific cancer-targeting properties. Herein, we have developed a nanocarrier system based on albumin, which selectively affects the tumor cells, and hence can revolutionize breast cancer therapy. The developed nanoparticles could be further used for the delivery of other hydrophobic drugs like SN38, which broadens the use of this system in the treatment of breast cancer.Albumin-based nanoparticles are an emerging platform for the delivery of various chemotherapeutics because of their biocompatibility, safety, and ease of surface modification for specific targeting. The most widely used method for the preparation of albumin nanoparticles is by desolvation process using glutaraldehyde (GLU) as a cross-linker. However, limitations of GLU like toxicity and interaction with drugs force the need for alternative cross-linkers. In the present study, several cross-linking systems were evaluated for the preparation of Bovine Serum Albumin (BSA) nanoparticles (ABNs) encapsulating Doxorubicin (Dox). Based on the results obtained from morphological characterization, in vitro release, and therapeutic efficacy in cells, N-succinimidyl 3-(2-pyridyldithio) propionate (SPDP)-modified ABNs (ABN-SPDP) was chosen. Since ABN-SPDP are formed with disulfide linkage, the drug release is facilitated under a highly reducing environment present in the tumor sites. The cytotoxicity studies of those ABN-SPDP were performed in three different breast cell lines, highlighting the mechanism of cell death. The Dox-encapsulated ABN-SPDP showed toxicity in both the breast cancer cells (MCF-7 and MDA-MB-231), but, remarkably, a negligible effect was observed in non-tumoral MCF-10A cells. In addition to the hydrophilic Dox, this system could be used as a carrier for hydrophobic drugs like SN38. The system could be employed for the preparation of nanoparticles based on human serum albumin (HSA), which further enhances the feasibility of this system for clinical use. Hence, the albumin nanoparticles developed herein present an excellent potential for delivering various drugs in cancer therapy.

Facile and scalable preparation of bovine serum albumin stabilized cobalt sulfide nanostructures with various morphologies

We present a protein-assisted method for the facile and scalable synthesis of Cobalt sulfide (CoS) nanostructures with various morphologies using bovine serum albumin (BSA) as a stabilizing agent. The CoS samples prepared from 10:1 volume ratio of Cobalt (Co):Sulfur (S) and 1:10 volume ratio of Co:S at 0.01% w/v amount of BSA shows 3D flowers with an average diameter of 510 nm and hollow spheres about 900 nm in average diameter, respectively. The CoS samples prepared from 0.01, 0.1 and 0.5% w/v amounts of BSA at 1:1 volume ratio of Co:S shows nanosheet based porous clusters, nanosheet based partially porous clusters and aggregated spheres, respectively. Fourier transform infrared spectroscopy study confirms that the obtained BSA stabilized CoS nanostructures are stabilized by hydroxyl and amine groups present in the BSA molecules.

Detection of Six β-Agonists by Three Multiresidue Immunosensors Based on an Anti-bovine Serum Albumin-Ractopamine-Clenbuterol-Salbutamol Antibody.

According to an indirect competitive immunoassay, six β-agonists (clenbuterol (CL), salbutamol (SAL), ractopamine (RAC), terbutaline (TER), mabuterol (MAB), and tulobuterol (TUL)) were detected by three novel multiresidue immunosensors on the basis of the successful preparation of bovine serum albumin (BSA)-RAC-CL-SAL multideterminant antigen and anti-BSA-RAC-CL-SAL antibody. A new strategy was reported to detect six β-agonists by combining nanotechnology, electrochemical detection, and specific immune technology. At the same concentration, the amperometric response for detection of six β-agonists was in a sequence of GCE/GNP/SAL > GCE/GNP/RAC > GCE/GNP/CL. Detection limits of six β-agonists show that the multiresidue detection performance of the GCE/GNP/RAC immunosensor is better than those of GCE/GNP/SAL and GCE/GNP/CL immunosensors. Three immunosensors manifest superior properties with a wide linear range, low detection limit, excellent reproducibility, and stability. The proposed GCE/GNP/RAC immunosensor displays high accuracy and can be effectively used for real sample detection.

Synthesis, photophysical and photobiological characterization of BSA nanoparticles loaded with chloroaluminium phthalocyanine by one-step desolvation technique for photodynamic therapy action

This work describes the preparation of bovine serum albumin (BSA) nanoparticles by one-step desolvation method using acetone/ethanol as precipitating agent, glutaraldehyde as crosslinking agent, sodium azide as a preservative and water as reaction media for chloroaluminium phthalocyanine (ClAlPc) incorporation for photodynamic therapy action. The characterization of the nanoparticulate system was carried out using steady-state technique, scanning electron microscopy study and their biological activity was evaluated using in vitro macrophages cell lines by classical MTT assay. All the spectroscopy measurements demonstrated good photophysical properties and the in vitro cytotoxicity study showed that the system is not cytotoxic in the darkness, but it exhibits a substantial phototoxicity at 0.90 mol.L−1 of photosensitizer concentration and 10.0 J cm−2 of light. These conditions are sufficient to kill about 90% of the cells. The results allowed us to conclude that ClAlPc-loaded in BSA nanoparticles might have potential application on drug delivery system for PDT protocols.

Preparation of bovine serum albumin molecularly imprinted polymer by precipitation polymerization

Through precipitation polymerization approach, bovine serum albumin (BSA) molecularly imprinted polymer (MIP) was synthesized with various reagents to ascertain the optimal synthesis condition. The optimized synthesis condition is methacrylic acid (MAA) as functional monomer, N,N′-methylenebisacrylamide (MBA) as crosslinker, template molecular/functional monomer/initiator ratio of 1:6:3, and K2S2O8/NaHSO3 initiator ratio of 1:2. BSA adsorption by synthesized MIP conformed to second-order kinetic adsorption equation and Langmuir adsorption isotherm. The maximum adsorption amount of MIP was 106.2 mg/g. Moreover, when the lysozyme (LYZ) was introduced as interfering adsorbate, the separation factor was up to 3.09, indicating that the MIP has a high affinity towards BSA.

Ex-situ Generation of the Gold Nanowire Networks Bovine Serum Albumin Bio-Conjugated System Using Pulsed Laser Ablation in a Harsh Environment

The experimental conditions were investigated to fabricate gold nanowire networks (AuNNWs) by pulsed laser ablation in saline solutions. The study revealed that the production of alternative nanoparticles (or aggregates) or nanowire networks at the fundamental wavelength of a Nd:YAG laser (1064 nm) depend on the medium media surrounding Au nanoparticles during the process of synthesis. The aggregates and precipitates of the gold nanoparticles (AuNPs) in saline solutions were caused by the harsh environment of the anions with Na+ cations in the solution. The ex-situ was used for the preparation of bovine serum albumin (BSA) bio-conjugates. Enhanced colloidal stability was dramatically achieved when BSA was adsorbed onto Au nanowire networks. The optical extinction spectra of the colloids in the UV/vis region were obtained to evaluate the structure of the dispersed Au phase. Transmission electron microscopy (TEM) was applied to visualize the size and morphology of the colloidal particles. Au nanowire networks compatibility can be prepared and applied in real environments.

Protein-Based Nanoparticle Preparation via Nanoprecipitation Method.

Nanoparticles are nowadays largely investigated in the field of drug delivery. Among nanoparticles, protein-based particles are of paramount importance since they are natural, biodegradable, biocompatible, and nontoxic. There are several methods to prepare proteins containing nanoparticles, but only a few studies have been dedicated to the preparation of protein- based nanoparticles. Then, the aim of this work was to report on the preparation of bovine serum albumin (BSA)-based nanoparticles using a well-defined nanoprecipitation process. Special attention has been dedicated to a systematic study in order to understand separately the effect of each operating parameter of the method (such as protein concentration, solvent/non-solvent volume ratio, non-solvent injection rate, ionic strength of the buffer solution, pH, and cross-linking) on the colloidal properties of the obtained nanoparticles. In addition, the mixing processes (batch or drop-wise) were also investigated. Using a well-defined formulation, submicron protein-based nanoparticles have been obtained. All prepared particles have been characterized in terms of size, size distribution, morphology, and electrokinetic properties. In addition, the stability of nanoparticles was investigated using Ultraviolet (UV) scan and electrophoresis, and the optimal conditions for preparing BSA nanoparticles by the nanoprecipitation method were concluded.

In situ preparation of water-soluble ginsenoside Rh2-entrapped bovine serum albumin nanoparticles: in vitro cytocompatibility studies.

The present study investigates a simple and convenient one-step procedure for the preparation of bovine serum albumin (BSA)-Rh2 nanoparticles (NPs) at room temperature. In this work, ginsenoside Rh2 was entrapped within the BSA protein to form BSA-Rh2 NPs to enhance the aqueous solubility, stability, and therapeutic efficacy of Rh2. The physiochemical characterization by high-performance liquid chromatography, nuclear magnetic resonance, Fourier transform infrared spectroscopy, field emission transmission electron microscopy, dynamic light scattering, and thermogravimetric analysis confirmed that the prepared BSA-Rh2 NPs were spherical, highly monodispersed, and stable in aqueous systems. In addition, the stability of NPs in terms of different time intervals, pHs, and temperatures (20°C–700°C) was analyzed. The results obtained with different pHs showed that the synthesized BSA-Rh2 NPs were stable in the physiological buffer (pH 7.4) for up to 8 days, but degraded under acidic conditions (pH 5.0) representing the pH inside tumor cells. Furthermore, comparative analysis of the water solubility of BSA-Rh2 NPs and standard Rh2 showed that the BSA nanocarrier enhanced the water solubility of Rh2. Moreover, in vitro cytotoxicity assays including cell viability assays and morphological analyses revealed that Rh2-entrapped BSA NPs, unlike the free Rh2, demonstrated better in vitro cell viability in HaCaT skin cell lines and that BSA enhanced the anticancer effect of Rh2 in A549 lung cell and HT29 colon cancer cell lines. Additionally, anti-inflammatory assay of BSA-Rh2 NPs and standard Rh2 performed using RAW264.7 cells revealed decreased lipopolysaccharide-induced nitric oxide production by BSA-Rh2 NPs. Collectively, the present study suggests that BSA can significantly enhance the therapeutic behavior of Rh2 by improving its solubility and stability in aqueous systems, and hence, BSA-Rh2 NPs may potentially be used as a ginsenoside delivery vehicle in cancer and inflammatory cell lines.

Immobilization of BSA on ionic liquid functionalized magnetic Fe3O4 nanoparticles for use in surface imprinting strategy

Combining template immobilization with surface imprinting technology is an effective strategy to overcome the difficulties associated with macromolecular template removal and to achieve high specific recognition ability. In this work, ionic liquid functionalized Fe3O4 nanoparticles were prepared via a simple two-step modification process and were used as substrate to immobilize bovine serum albumin (BSA). The zeta potential study revealed immobilization of BSA on the nanoparticles through multiple interactions, and the immobilization capacity was about nine times higher compared with that of bare Fe3O4. Subsequently, dopamine was utilized as functional monomer to prepare BSA surface imprinted nanoparticles. Fourier transform infrared spectroscopy, thermo-gravimetric analysis and transmission electron microscopy verified the successful preparation of BSA imprinted nanoparticles with core-shell structure. The influence of imprinted layer thickness on recognition ability of imprinted nanoparticles was investigated, and the results suggested that 20nm was an optimum thickness to achieve the best recognition ability. The adsorption isotherm studies showed that the imprinted nanoparticles had a significantly higher adsorption capacity and stronger binding affinity than the non-imprinted ones. Furthermore, the selective as well as the competitive adsorption studies revealed higher selectivity and recognition ability of the imprinted nanoparticles for BSA. Therefore, the proposed strategy is an effective way to obtain protein imprinted polymers with high adsorption capacity and good recognition ability, thus would be beneficial for the further development and application of protein imprinting technology.

Preparation of protein imprinted microspheres using amphiphilic ionic liquid as stabilizer and emulsifier via miniemulsion polymerization

Design and preparation of functional materials for selective recognition of biomacromolecules such as proteins, DNA, viruses, and bacteria have always been extremely challenging due to their structure sensitivity. Regrettably, the structure stability of biomacromolecules in molecularly imprinted technology was rarely addressed. This paper presents an effective procedure for the facile preparation of bovine serum albumin (BSA) interfacial molecularly imprinted microspheres (IMIMs), using an imidazole-based amphiphilic ionic liquid (IL), which played a dual role of a stabilizer and emulsifier, via miniemulsion polymerization at 25°C. In order to prove the stabilizing effect of IL on BSA, a conventional emulsifier sodium dodecyl sulfate (SDS), was also used as the emulsifier for comparison. Different characterization methods were employed to investigate the stability of BSA structure and track the experimental process. The results reveal that the destruction of structure of BSA by amphiphilic IL, 1-dodecyl-3-methylimidazolium chloride ([DMM]Cl), was much lower than that by SDS. Moreover, good selectivity of IMIMs-[DMM]Cl towards BSA was certified in the batch-wise and selectivity rebinding tests, in which an imprinting factor of 3.32 was obtained. This was superior to IMIMs-SDS and demonstrated to be a promising platform for recognition of protein with good specificity.

Pulmonary Delivery of Proteins Using Nanocomposite Microcarriers

In this study, Taguchi design was used to determine optimal parameters for the preparation of bovine serum albumin (BSA)-loaded nanoparticles (NPs) using a biodegradable polymer poly(glycerol adipate-co-ω-pentadecalactone) (PGA-co-PDL). NPs were prepared, using BSA as a model protein, by the double emulsion evaporation process followed by spray-drying from leucine to form nanocomposite microparticles (NCMPs). The effect of various parameters on NP size and BSA loading were investigated and dendritic cell (DC) uptake and toxicity. NCMPs were examined for their morphology, yield, aerosolisation, in vitro release behaviour and BSA structure. NP size was mainly affected by the polymer mass used and a small particle size ≤500 nm was achieved. High BSA (43.67 ± 2.3 μg/mg) loading was influenced by BSA concentration. The spray-drying process produced NCMPs (50% yield) with a porous corrugated surface, aerodynamic diameter 1.46 ± 141 μm, fine particle dose 45.0 ± 4.7 μg and fine particle fraction 78.57 ± 0.1%, and a cumulative BSA release of 38.77 ± 3.0% after 48 h. The primary and secondary structures were maintained as shown by sodium dodecyl sulphate poly (acrylamide) gel electrophoresis and circular dichroism. Effective uptake of NPs was seen in DCs with >85% cell viability at 5 mg/mL concentration after 4 h. These results indicate the optimal process parameters for the preparation of protein-loaded PGA-co-PDL NCMPs suitable for inhalation.

Synthesis of biologically active cadmium (II) complex with tridentate N2O donor Schiff base: DFT study, binding mechanism of serum albumins (bovine, human) and fluorescent nanowires

The photophysical properties of luminescent tetra-coordinated cadmium (II) complex formulated as [Cd(L)Cl],HL=(1-[(3-methyl-pyridine-2-ylimino)-methyl]-naphthalen-2-ol) were synthesized and characterized by analytical and spectroscopic methods. The density function theory calculations are used to investigate the electronic structures of the ligand and its complex. The interactions of cadmium (II) complex towards bovine serum albumin (BSA) and human serum albumin (HSA) were investigated using absorption and fluorescence spectroscopic techniques at pH 7.4. The quenching constants, binding constants and number of binding sites were determined by fluorescence quenching method. The calculated thermodynamic parameters (ΔG, ΔH, and ΔS) confirmed that the binding reaction is mainly entropy-driven and hydrophobic forces played an important role in the reaction. Here, we proposed a new synthetic procedure for the preparation of BSA and HSA with cadmium complex nanowires. The scanning electron microscopy images show that BSA and HSA with cadmium complex product are wire-like in structure. The complex shows enhanced antibacterial activity compared with the free ligand and standard antibiotic chloramphenicol. Antioxidant studies showed that the complex has significant antioxidant activity against DPPH. The obtained IC50 value of the DPPH activity for complex (IC50=138μg/ml) showed excellent scavenging property compared to standard ascorbic acid.

In vitro evaluation of potential complexation between bovine insulin and bovine serum albumin

The objective of this study was to examine the possible binding of bovine insulin (BI) with bovine serum albumin (BSA) to form a new potential diabetogenic irreversible complex protein. Several preparations of BSA and BI were prepared. Both capillary electrophoresis and spectrophotometric analysis were undertaken to test the possibility of complexation between BI and BSA. HPLC was used to test whether the potential complex of BI and BSA is reversible or irreversible. The optimum deviation between the real and calculated absorbances was observed at a BI/BSA ratio of 2. Moreover, the migration time of BI decreased substantially with increasing ratio of BI to BSA until it became almost constant at equal molar ratio of BI/BSA. While the majority of the 2:1 BI-BSA sample detached during the HPLC analysis, which confirms the reversible character of BI-BSA binding, the HPLC chromatogram also emphasizes the formation of an irreversible complexation between the two proteins. This study provides evidence of the formation of reversible and irreversible new BI-BSA complexes under physiological conditions. This highlights the importance of examining the possible diabetogenicity of BI-BSA complex in genetically susceptible people.

Preparation of Bovine Serum Albumin (BSA) nanoparticles by desolvation using a membrane contactor: A new tool for large scale production

Albumin nanoparticles are attractive drug delivery systems as they can be prepared under soft conditions and incorporate several kinds of molecules. The aim of this study was to upscale the desolvation process for preparing Bovine Serum Albumin (BSA) nanoparticles using a membrane contactor. At a first step, the BSA nanoparticles were prepared at small scale using a syringe pump. BSA nanoparticles of 139nm in size, with a polydispersity index of 0.046, were obtained at the optimal conditions: pH 8.2, 100mgmL−1 BSA albumin solution (2mL), and 1mLmin−1 flow rate of ethanol addition (8mL). The upscaling with a membrane contactor was achieved by permeating ethanol through the pores of a Shirasu Porous Glass (SPG Technology Co., Japan) membrane and circulating the aqueous phase tangentially to the membrane surface. By increasing the pressure of the ethanol from 1 to 2.7 bars, a progressive decrease in nanoparticle size was obtained with a high nanoparticles yield (around 94–96%). In addition, the flow rate of the circulating phase did not affect the BSA nanoparticle characteristics. At the optimal conditions (pH 8.2, 100mgmL−1 BSA albumin solution, pressure of ethanol 2.7 bars, flow rate of the circulating phase 30.7mLs−1), the BSA nanoparticles showed similar characteristics to those obtained with the syringe pump. Large batches of BSA nanoparticles were prepared up to 10g BSA. The BSA nanoparticles were stable at least during 2months at 4°C, and their characteristics were reproducible. It was then concluded that the membrane contactor technique could be a suitable method for the preparation of albumin nanoparticles at large scale with properties similar to that obtained at small scale.

Synthesis of fluorescent BSA–Au NCs for the detection of Hg2+ ions

In this study, we present a simple heating approach for preparation of gold nanoclusters (Au NCs) using bovine serum albumin (BSA) as a template. At 70 °C, the reaction for the preparation of BSA–Au NCs is completed within 20 min. By conducting matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS), we have found that the main product is BSA–Au20 NCs that emit at 660 nm when excited at 330 nm due to “molecular-like” behavior. The X-ray photoelectron spectroscopy data reveal that there are Au+ ions and Au atoms coexisting in the BSA–Au NCs. The as-prepared Au NCs show excellent stability over a wide pH range (2.0–10.0). The fluorescence and MALDI-MS data reveal that the changes in their fluorescence properties are due to the formation of various sizes of BSA–Au NCs for different periods of reaction time. The as-prepared BSA–Au NCs are selective and sensitive (limit of detection of 4 nM at a signal-to noise ratio 3) for the detection of Hg2+ ions through the d10–d10 metallophilic interaction of Au+ and Hg2+ that leads to a decrease in fluorescence. The present assay has been validated for the detection of Hg2+ ions in real water samples, with a result being in good agreement with that from inductively coupled plasma mass spectrometry.

Enzyme-linked immunosorbent assay (ELISA) and blocking with bovine serum albumin (BSA)—not all BSAs are alike

The enzyme-linked immunosorbent assay (ELISA) is an extremely common and powerful laboratory technique for detecting proteins by antibodies. Researchers frequently use bovine serum albumin (BSA) as a blocking agent to prevent non-specific binding of antigens and antibodies to the microtiter well. While studying the interactions of the vaccinia virus complement control protein (VCP) with complement, we found non-specific binding of VCP to BSA and identify a BSA preparation that did not result in non-specific binding. This work draws attention to the fact that not all BSA preparations are alike. It also highlights the need to perform critical controls to ensure that ELISA reactants do not inappropriately bind to the blocking agent.

Preparation of bovine serum albumin immobilized adsorbent for specific adsorption of bilirubin

Serum bilirubin concentration is greatly elevated in certain diseases such as hyperbilirubinemia and severe hepatitis. Lowering the level of bilirubin is one of the major targets of many therapies such as plasma exchange and hemoperfusion. In this study, a bilirubin specific adsorbent was prepared by covalently immobilizing bovine serum albumin (BSA) onto macroporous poly (glycidyl methacrylate-co-trimethylolpropane trimethacrylate) microspheres. The resulting BSA immobilized adsorbent (BIA) demonstrated good performance in adsorption of bilirubin with an adsorption capacity of 48.7 mg/g. Presence of BSA in bilirubin solution significantly lowered the adsorption capacity of the adsorbent due to the tight binding of bilirubin onto BSA. Adsorption performance of the adsorbent for bilirubin was improved with the elevation of temperature. The adsorbent demonstrated good stability even after 31 d of storage at - 80 degrees C in that there was almost no change in adsorption capacity for bilirubin. These results indicated that the prepared BSA immobilized adsorbent could be an alternative choice for specific adsorption of bilirubin.

Specific rebinding property of protein macromolecularly imprinted polymer microspheres based on calcium alginate hydrogel via gas jetting‐dropping method

AbstractAlginate hydrogel polymer microspheres are usually prepared by inverse suspending method. The main problem is the remained suspending medium and surfactant on the beads. Syringe dropping or extruding method avoids using of the organic solvents. However, it is difficult to control the particle dimension and produce in large quantity. We have developed a new method called nitrogen gas jetting‐dropping (GJD) method for the preparation of bovine serum albumin (BSA) imprinted polymer microspheres based on calcium alginate hydrogel. The microspheres can be produced continuously without using any hydrophobic medium or surfactant. The particle diameter is controlled by adjusting pressure and needle dimension. BSA‐imprinted alginate microspheres were prepared by the GJD method and the rebinding tests were investigated. The equilibrium rebinding capacity ranged from 0.01 to 0.014 μmol/g. The imprinting efficiency towards BSA was from 1.46 to 2.17 with the greatest separation factor of 1.523 against a contrastive template ovalbumin (OVA). © 2010 Wiley Periodicals, Inc. J Appl Polym Sci, 2010

On the mechanical properties of bovine serum albumin (BSA) adhesives

Biological adhesives, natural and synthetic, are of current active interest. These adhesives offer significant advantages over traditional sealant techniques, in particular, they are easier to use, and can play an integral part in the healing mechanism of tissue. Thus, biological adhesives can play a major role in medical applications if they possess adequate mechanical behavior and stability over time. In this work, we report on the method of preparation of bovine serum albumin (BSA) into a biological adhesive. We present quantitative measurements that show the effect of BSA concentration and cross-linker content on the bonding strength of BSA adhesive to wood. A comparison is then made with synthetic poly(glycidyl methacrylate) (PGMA) adhesive, and a commercial cyanoacrylate glue, which was used as a control adhesive. In addition, BSA samples were prepared and characterized for their water content, tensile strength, and elasticity. We show that on dry surface, BSA adhesive exhibits a high bonding strength that is comparable with non-biological commercial cyanoacrylate glues, and synthetic PGMA adhesive. Tensile testing on wet wood showed a slight increase in the bonding strength of BSA adhesive, a considerable decrease in the bonding strength of cyanoacrylate glue, and negligible adhesion of PGMA. Tests performed on BSA samples demonstrate that initial BSA concentration and final water content have a significant effect on the stress-strain behavior of the samples.