Bovine Serum Albumin Surface Research Articles

Preparation of pure phase silver nanoparticles: Morphological, optical, binding interactions with bovine serum albumin and antioxidant potential studies

Pure silver nanoparticles (AgNPs) were synthesized using Senecio madagascariensis plant extract and oleic acid as capping agents. The powder X-ray diffraction patterns of the silver nanoparticles were indexed to the face-centred cubic phase of Ag. TEM images of the nanoparticles revealed polydisperse spherical nanoparticles with particle size of 9 to 22 nm range. The GC-MS revealed terpenes as some phytochemicals extracted, which the FTIR bands corroborated. The results confirmed that increase in oleic acid concentration increased the size of the silver nanoparticles. The nanoparticles' optical band gaps, Eg, were 2.26 – 2.56 eV, which decreased with particle size. The AgNPs exhibited potential antioxidant activity, as demonstrated by the DPPH scavenging assay. The DPPH scavenging activity was highest, with AgNP1 at 80 % and an IC50 of 1.668 μg/mL. Fluorescence and ultraviolet (UV) titrations were used to study the interaction of the silver nanoparticles (AgNP1) with bovine serum albumin (BSA). The Kapp value of the AgNP1 was calculated to be 3.14 × 104 ± 0.02 Lmol−1, KSV calculated as 7.38 × 104 ± 0.12 M−1. In the study, AgNPs bind to BSA potentially through a static quenching mechanism with one binding site that leads to developing a ground state complex. It is proposed that AgNPs bond to BSA's surface spontaneously based on its thermodynamic characteristics and binding constants.

Drug Binding to Partially Unfolded Serum Albumin: Insights into Nonsteroidal Anti-Inflammatory Drug Naproxen-BSA Interactions from Spectroscopic and MD Simulation Studies.

Understanding the binding details of a small-molecule drug to a protein in its partially unfolded state is important for drug delivery as it provides insight into the overall drug-binding ability of the protein, even when the majority of binding pockets in its unfolded state are impaired. The interaction of partially unfolded proteins with drugs remains poorly understood due to a lack of structural information on proteins in their partially unfolded states. Here, we studied the interaction between serum albumin (bovine serum albumin (BSA) as a model system), an abundant protein in blood serum that is an effective carrier for numerous known drugs, and a nonsteroidal anti-inflammatory drug (NSAID) naproxen (NPS) using various spectroscopic and computational methods. Molecular dynamics simulations starting from the drug-unbound state and performed at physiological and higher temperatures revealed novel hydrophobic sites on the BSA surface. We analyzed the BSA-NPS interaction in the presence and absence of the cationic organized assembly CTAB and two oligosaccharides (β-CD and 2-HP-β-CD) at different excitation wavelengths. The solvation dynamics of BSA under NPS-bound conditions became ∼4.6% faster. Oligosaccharides were found to increase the solubility of NPS by providing a hydrophobic environment for the formation of inclusion complexes through host-guest interactions. These findings provide a comprehensive overview and uncover the binding model and mechanism of interaction of NPS with BSA, revealing hydrophobic and electrostatic interactions and hydrogen bonds required for BSA to bind NPS at these noncanonical sites. The molecular-level understanding of the binding mechanism of commonly used NSAIDs like NPS with partially unfolded BSA will be useful in designing pharmaceutically important molecules with efficient loading and delivery properties.

Biodegradable copper-iodide clusters modulate mitochondrial function and suppress tumor growth under ultralow-dose X-ray irradiation

Both copper (Cu2+/+) and iodine (I−) are essential elements in all living organisms. Increasing the intracellular concentrations of Cu or I ions may efficiently inhibit tumor growth. However, efficient delivery of Cu and I ions into tumor cells is still a challenge, as Cu chelation and iodide salts are highly water-soluble and can release in untargeted tissue. Here we report mitochondria-targeted Cu-I cluster nanoparticles using the reaction of Cu+ and I− to form stable bovine serum albumin (BSA) radiation-induced phosphors (Cu-I@BSA). These solve the stability issues of Cu+ and I− ions. Cu-I@BSA exhibit bright radioluminescence, and easily conjugate with the emission-matched photosensitizer and targeting molecule using functional groups on the surface of BSA. Investigations in vitro and in vivo demonstrate that radioluminescence under low-dose X-ray irradiation excites the conjugated photosensitizer to generate singlet oxygen, and combines with the radiosensitization mechanism of the heavy atom of iodine, resulting in efficient tumor inhibition in female mice. Furthermore, our study reveals that BSA protection causes the biodegradable Cu-I clusters to release free Cu and I ions and induce cell death by modulating mitochondrial function, damaging DNA, disrupting the tricarboxylic acid cycle, decreasing ATP generation, amplifying oxidative stress, and boosting the Bcl-2 pathway.

Polyaniline-based bovine serum albumin imprinted electrochemical sensor for ultra-trace-level detection in clinical and food safety applications

Monitoring bovine serum albumin (BSA) at ultra-low levels is crucial for clinical and food safety applications, as it plays a significant role in identifying various health conditions and potential risks, necessitating fast, trace-level detection of BSA. This study proposes an approach to address these challenges by employing molecularly imprinted polymer (MIP) to develop an ultra-trace-level and cost-effective BSA sensing platform. The MIP electrochemical sensor was developed using polyaniline (PANI) combined with the protein crosslinker glutaraldehyde (GA) to optimize BSA surface imprinting in the MIP. As a result, the sensor achieves a sensitivity of 1.24 μA/log(pg/mL), with a picomolar detectable limit of 2.3 pg/mL (0.035 pM) and a wide detection range from 20 pg/mL to 200,000 pg/mL (0.303 pM to 3030 pM), making it suitable for clinical and food safety applications. Additionally, the study explores the interaction between an acidic surfactant protein eluent (acetic acid with sodium dodecyl sulfate, AcOH-SDS) and BSA vacant sites, enhancing recognition and re-binding. The PANI-based MIP sensor demonstrates initial feasibility and practicality in commercial milk and real human serum, opening avenues for early disease detection and ensuring food safety in BSA-related immune responses.

A Proline-Based Artificial Enzyme That Favors Aldol Condensation Enables Facile Synthesis of Aliphatic Ketones via Tandem Catalysis.

A proline-based artificial enzyme is prepared by grafting the l-proline moieties onto the surface of bovine serum albumin (BSA) protein through atom transfer radical polymerization (ATRP). The artificial enzyme, the BSA-PolyProline conjugate, prefers to catalyze the formation of unsaturated ketones rather than β-hydroxy ketones in the reaction between acetone and aldehydes, which is difficult to achieve in free-proline catalysis. The altered reaction selectivity is ascribed to the locally concentrated l-proline moieties surrounding the BSA molecule, indicating a microenvironmental effect-induced switching of the reaction mechanism. Taking advantage of this selectivity, we used this artificial enzyme in conjunction with a natural enzyme, old yellow enzyme 1 (OYE1), to demonstrate a simple synthesis of different aliphatic ketones from acetone and aldehydes via tandem catalysis.

Unveiling the Three-Step Model for the Interaction of Imidazolium-Based Ionic Liquids on Albumin.

The effect of the ionic liquids (ILs) 1-methyl-3-tetradecylimidazolium chloride ([C14MIM][Cl]), 1-dodecyl-3-methylimidazolium chloride ([C12MIM][Cl]), and 1-decyl-methylimidazolium chloride ([C10MIM][Cl]) on the structure of bovine serum albumin (BSA) was investigated by fluorescence spectroscopy, ultraviolet-visible (UV-vis) spectroscopy, small-angle X-ray scattering (SAXS), and molecular dynamics (MD) simulations. Concerning the fluorescence measurements, we observed a blue shift and a fluorescence quenching as the IL concentration increased in the solution. Such behavior was observed for all three studied imidazolium-based ILs, being larger as the number of methylene groups in the alkyl chain increased. UV-vis absorbance measurements indicate that even at relatively small IL/protein ratios, like 1:1 or 1:2, ([C14MIM][Cl]) is able to change, at least partially, the sample turbidity. SAXS results agree with the spectroscopic techniques and suggest that the proteins underwent partial unfolding, evidenced by an increase in the radius of gyration (Rg) of the scattering particle. In the absence and presence of ([C14MIM][Cl]) = 3 mM BSA Rg increases from 29.1 to 45.1 Å, respectively. Together, these results indicate that the interaction of BSA with ILs is divided into three stages: the first stage is characterized by the protein in its native form. It takes place for protein/IL ≤ 1:2, and the interaction is predominantly due to the electrostatic forces provided by the negative charges on the surface of BSA and the cationic polar head of the ILs. In the second stage, higher IL concentrations induce the unfolding of the protein, most likely inducing the unfolding of domains I and III, in such a way that the protein's secondary structure is kept almost unaltered. In the last stage, IL micelles start to form, and therefore, the interaction with protein reaches a saturation point and free micelles may be formed. We believe that this work provides new information about the interaction of ILs with BSA.

New insights into the pH dependence of anthocyanin-protein interactions by a case study of cyanidin-3-O-glucoside and bovine serum albumin

Anthocyanins are natural pigments that can undergo structural transformations depending on pH, and their interactions with proteins have received considerable attention in recent decades. This work intended to unravel the pH-dependence of anthocyanin-protein binding mechanisms by examining interactions between cyandin-3-O-glucoside (C3G) and bovine serum albumin (BSA) at different pH. Fluorescence quenching (FQ) and microscale thermophoresis (MST) demonstrated that their binding affinity was pH 7 > pH 5 > pH 3, with dissociation constant (Kd) at pH 7 of 43.1 μM for FQ and 33.0 μM for MST. The predominant C3G forms were determined by measuring UV–Vis absorption spectra with pH-jump experiments. Additionally, circular dichroism, Trp fluorescence, zeta potential and particle size measurements demonstrated the “molten globule” state of BSA at pH 3, and C3G had a negligible effect on BSA conformation. The binding mechanisms were investigated using molecular dynamics simulation, which revealed the importance of electrostatic interaction. Flavylium cation rarely bound to BSA due to electrostatic repulsion at pH 3, whereas the uncharged forms of C3G at all pH values bound to BSA surface due to hydrophobic interactions and hydrogen bonds, but possibly in a weak and nonspecific manner. Anionic quinoidal bases, the most common C3G forms at pH 7, mostly bound to the positively charged pockets of BSA and formed several hydrogen bonds with surrounding amino acids, resulting in higher binding affinity. These findings provide insights into the interactions of proteins with different anthocyanin forms, which may guide the future research and applications in this field.

Effect of protein adsorption on the dissolution kinetics of silica nanoparticles

Nanoparticulate systems in the presence of proteins are highly relevant for various biomedical applications such as photo-thermal therapy and targeted drug delivery. These involve a complex interplay between the charge state of nanoparticles and protein, the resulting protein conformation, adsorption equilibrium and adsorption kinetics, as well as particle dissolution. SiO2 is a common constituent of bioactive glasses used in biomedical applications. In this context, the dissolution behavior of silica particles in the presence of a model protein, bovine serum albumin (BSA), at physiologically relevant pH conditions was studied. Sedimentation analysis using an analytical ultracentrifuge showed that BSA in the supernatant solution is not affected by the presence of silica nanoparticles. However, zeta potential measurements revealed that the presence of the protein alters the particles’ charge state. Adsorption and dissolution studies demonstrated that the presence of the protein significantly enhances the dissolution kinetics via interactions of positively charged amino acids in the protein with the negative silica surface and interaction of BSA with dissolved silicate species. Our study provides comprehensive insights into the complex interactions between proteins and oxide nanoparticles and establishes a reliable protocol paving the way for future investigations in more complex systems involving biological solutions as well as bioactive materials.

Calixarene-modified albumin for stoichiometric delivery of multiple drugs in combination-chemotherapy.

Rationale: In combination chemotherapy, the molar ratio of drugs is a critical parameter that determines the synergistic effects. However, most co-delivery vectors are incapable of maintaining the optimal molar ratio of drugs throughout the delivery process. Herein, a calixarene-modified albumin (CaMA), which can co-deliver multiple drugs with precise control of the drug ratio, is presented.Methods: CaMA was prepared by chemically conjugating multiple sulfonate azocalix[4]arenes (SAC4A) onto the surface of bovine serum albumin (BSA). The precise drug loading and synchronous drug release were measured using fluorescence spectroscopy. Mouse tumor cell 4T1 and 4T1-bearing mice were used to evaluate the combined effects of mitomycin C (MMC) and doxorubicin (DOX) in vitro and in vivo.Results: With multiple hypoxia-responsive calixarenes conjugated onto a single albumin molecule, CaMA achieved precise drug loading and synchronous release of multiple drugs into the tumor microenvironment. This unique drug loading and release mechanism ensures that CaMA maintains the drug ratio from the initial drug loading to the release site, providing a solid foundation for multi-drug combination therapy with the goal of achieving predictable therapeutic outcomes in vivo. The delivery of the model drug combination MMC and DOX at a prescreened ratio via CaMA achieved significantly enhanced tumor suppression and reduced systemic toxicity.Conclusions: This stoichiometric delivery feature makes CaMA a powerful tool for the development of combination chemotherapy and personalized medications for cancer treatment.

Insights into the impacts of dissolved organic matter of different origins on bioaccumulation and translocation of per- and polyfluoroalkyl substances (PFASs) in wheat

Per- and polyfluoroalkyl substances (PFASs) have been found to be widely present in soil. Dissolved organic matter (DOM) in soil are supposed to greatly affect the bioavailability of PFASs in soil. Herein, hydroponic experiments were conducted to understand the impacts of two kinds of typical DOM, bovine serum albumin (BSA) and humic acid (HA), on the uptake and translocation of legacy PFASs and their emerging alternatives, perfluorooctane sulfonic acid (PFOS), perfluorooctane acid (PFOA), perfluorohexane sulfonic (PFHxS) and 6:2 chlorinated polyfluoroalkyl ether sulfonate (6:2 Cl-PFESA) in wheat (Triticum aestivum L.). The results indicated that both HA and BSA significantly inhibited the bioaccumulation and translocation of PFASs in the roots and shoots of wheat, and the impacts of BSA were greater than HA. This difference was explained by the greater binding affinities of the four PFASs with BSA than with HA, as evidenced by the equilibrium dialysis and isothermal titration calorimetry (ITC) analyses. It was noting that inhibition impacts of the BSA-HA mixture (1:1) were lower than BSA alone. The results of Fourier transform infrared (FT-IR) spectroscopy and excitation-emission matrix (EEM) fluorescence spectroscopy suggested that HA could bind with the fluorescent tryptophan residues in BSA greatly, competing the binding sites with PFASs and forming a cover on the surface of BSA. As a result, the binding of PFASs with BSA-HA complex was much lower than that with BSA, but close to HA. The results of this study shed light on the impacts of DOM in soil on the bioaccumulation and translocation of PFASs in plants.

Radioprotective Role of Vitamins C and E against the Gamma Ray-Induced Damage to the Chemical Structure of Bovine Serum Albumin.

Radioprotective effects of vitamin C and vitamin E as a water-soluble and a lipid-soluble agent, respectively, were investigated at the molecular level during the imposition of gamma radiation-induced structural changes to bovine serum albumin (BSA) at the therapeutic dose of 3 Gy. Secondary and tertiary structural changes of control and irradiated BSA samples were investigated using circular dichroism and fluorescence spectroscopy. The preirradiation tests showed nonspecific and reversible binding of vitamins C and E to BSA. Secondary and tertiary structures of irradiated BSA considerably changed in the absence of the vitamins. Upon irradiation, α-helices of BSA transitioned to beta motifs and random coils, and the fluorescence emission intensity decreased relative to nonirradiated BSA. In the presence of the vitamins C or E, however, the irradiated BSA was protected from these structural changes caused by reactive oxygen species (ROS). The two vitamins exhibited different patterns of attachment to the protein surface, as inspected by blind docking, and their mechanisms of protection were different. The hydrophilicity of vitamin C resulted in the predominant scavenging of ROS in the solvent, whereas hydrophobic vitamin E localized on the nonpolar patches of the BSA surface, where it did not only form a barrier for diffusing ROS but also encountered them as an antioxidant and neutralized them thanks to the moderate BSA binding constant. Very low concentrations of vitamins C or E (0.005 mg/mL) appear to be sufficient to prevent the oxidative damage of BSA.

Rapid synthesis of fluorescent bovine serum albumin-gold nanoclusters complex for glutathione determination.

A facile one-pot method for synthesis of bovine serum albumin (BSA)-gold nanoclusters (AuNCs) has been developed. The formation of BSA-AuNCs took only 30s under mild conditions. BSA-AuNCs exhibited strong orange-yellow fluorescence, and the excitation and emission peaks were at 370nm and 564nm, respectively. In the process of forming BSA-AuNCs, the molecular chain of BSA has not been destroyed. Moreover, there were a large number of Au cations on the surface of BSA-AuNCs, which had strong oxidizing abilities. The reason for the ultrabright fluorescence of BSA-AuNCs was attributed to the Au(0)@Au(I)@Au(III)-ligand structure on the surface of BSA. In order to evaluate the fluorescence performance of BSA-AuNCs, BSA-AuNCs was used as a probe, realizing the sensitive and selective determination of glutathione (GSH) in a wide linear range of 0.01-0.48μM and a detection limit of 3.3nM. The proposed method not only offers a brand-new scheme for synthesizing BSA-AuNCs, but also provides a platform for studying the interaction between metal core and proteins. A facile one-pot method to synthesize ultrabright fluorescent BSA-AuNCs in tens of seconds has been introduced by mixing BSA suspension, KSCN, and HAuCl4. The as-prepared BSA-AuNCs showed intensive orange-yellow fluorescence under a UV lamp (365nm), and BSA still keeps the integral molecular chains during the whole synthesis process. Moreover, the as-prepared BSA-AuNCs have realized the sensitive and selective detection of glutathione (GSH) in a wide linear range of 0.01-0.48μM and a detection limit of 3.3nM.

Improving detection of BSA protein by applying atmospheric pressure plasma jets in MALDI-TOF mass spectrometry

To enhance protein identification in mass spectrometry systems, plasma can be applied in the sample preparation step in addition to conventional use, which improves the ionization process. In the present study, cold plasma technology is evaluated to achieve highly sensitive detection of low analyte concentrations.Plasma treatments are performed by two different low-temperature atmospheric-pressure sources. The protein ion signal after plasma treatment is characterized by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS). The sample preparation method, exposure time and gas type for bovine serum albumin (BSA) are optimized. Plasma characteristics are determined by optical emission spectroscopy (OES) method. Also, the temperatures of plasma environment and sample are measured during the treatment with a non-contact infra-red digital camera.The water-soluble BSA protein is irradiated by cold atmospheric-pressure plasma jet (CAP jet) and radio-frequency plasma jet (RF jet). Mass spectra showed that argon plasma treatment with two-layer method induced a significant increase in ion intensity of MALDI-TOF MS. Argon treated water-soluble BSA and powder BSA lead to ten-times and three-times enhancement of protein ion signals as compared to the control, respectively. Also, treatment with argon RF jet, increases the ion signal more than two-times.The results indicate that ion intensity of BSA treated with CAP jet is significantly higher than that of BSA treated with RF jet. This finding, in addition to frequency and geometry parameters, depends on more analyte protonation, resulting in more ion flux toward BSA surface. Further, two-layer technique is considered as an optimal sampling method for MALDI.

Interaction between bovine serum albumin and Solutol® HS 15 micelles: A two-stage and concentration-dependent process

The objective of this study was to investigate the interaction and the time evolution between protein and nanomicelles and to further understand the interaction mechanisms. Solutol® HS 15 (HS 15) and bovine serum albumin (BSA) were selected as the model nanomicelles and model protein, respectively. HS 15 has been used as solubilizer for injection, oral and subcutaneous administration systems. BSA was chosen as the model protein for its high sequence similarity and homology to human serum albumin. The interaction between BSA and HS 15 was studied by particle size distribution and zeta-potential measurement and fluorescence quenching assay. The effects of HS 15 concentration on the interaction between HS 15 nanomicelles and protein were investigated. The interaction mechanisms between BSA and HS 15 was studied by isothermal titration calorimetry and molecular docking. The interaction between HS 15 and BSA was demonstrated to be a two-stage process, with 0–3 h as the first phase and 3–12 h as the second phase. Moreover, the rearranged capsule-shaped HS 15 micelles could be absorbed onto the surface of BSA and the binding mode between HS 15 and BSA was concentration-dependent. Additionally, the interaction mechanisms of HS 15 and BSA include van der Waals forces, hydrophobic forces, and hydrogen bonding. In conclusion, this study provided a detailed study and insights of the interactions between nanomicelles and the serum albumin in vitro, which is of high importance to predict and understand the in vivo fate of such micellar drug delivery systems after intravenous injection in the future study.

Surface chemistry of bovine serum albumin with hematite nanoparticles and its effect on arsenate adsorption

Environmental context Hematite nanoparticles are efficient adsorbents for proteins and pollutants in environmental and biological systems. Hematite and the protein bovine serum albumin (BSA) were used as models to investigate the surface chemistry and competitive role of BSA in arsenate adsorption. Results show that surface BSA inhibits arsenate adsorption, potentially altering its mobility and bioavailability. Abstract The surface chemistry of metal oxide nanomaterials controls their health impacts and fate in environmental and biological systems. These systems contain proteins capable of binding to nanoparticles, which forms a protein corona that modifies the surface properties of the nanoparticles and reactivity towards pollutants. Using attenuated total reflectance-Fourier transform infrared (ATR-FTIR) spectroscopy, we investigate the adsorption of bovine serum albumin (BSA) and quantify the competitive effect of BSA on the adsorption kinetics of arsenate, AsV, to hematite nanoparticles. Experiments were conducted in the flow mode at pH 7. BSA was first adsorbed on hematite, then AsV was allowed to flow over the BSA/hematite thin film. Adsorption kinetic and thermodynamic parameters were calculated using a modified Langmuir adsorption model for both BSA and AsV. The adsorption thermodynamic model showed that BSA binds through two active sites with a binding energy of –41 kJ mol−1, which corresponds to the spontaneous formation of chemisorbed and physisorbed species. When AsV flowed over the BSA/hematite film, only 11 % of surface BSA was desorbed by AsV. This result highlights the inhibitory effect of BSA for AsV adsorption. Structural analysis of BSA revealed changes to the local conformational geometry upon adsorption to and desorption from hematite nanoparticles. Molecular docking simulations showed that the binding free energy of a modelled hematite nanoparticle towards the BSA surface is –6.8 kcal mol−1 (−28.5 kJ mol−1) owing to the formation of various bonds, which agrees with the adsorption kinetics modelling. Overall, surface BSA inhibits arsenate adsorption and therefore increases its mobility and bioavailability.

Osmotic pressure and transport coefficient in ultrafiltration: A Monte Carlo study using quantum surface charges

The calculation of the Osmotic Pressure and the Diffusion Coefficient, characterizing the cake layer developing during the Ultrafiltration (UF) of Bovine Serum Albumin (BSA), through a Multiscale Model based on Quantum Mechanics (QM) and Monte Carlo methods (MC) was the aim of this work. From the ab-initio results described in previous works, the distribution of the BSA surface charges was used. A home-made Metropolis MC algorithm, aimed at simulating the formation of BSA loose or concentrated layers during membrane operations, was also implemented. In such a MC algorithm, a DLVO energy calculation methodology of the adsorbed system was developed. Different MC simulations and Hypernetted Chain theory (HNC) calculations were performed so to determine both the Osmotic Pressure and the Diffusion Coefficient of BSA according to the Chun and Bowen approach, thus allowing a comparison between the calculated values of osmotic pressure and a set of experimental data taken from the literature. Such a comparison showed a good agreement between the simulated and the experimental results.

The Role of Surface Properties on Protein Aggregation Behavior in Aqueous Solution of Different pH Values.

This study aimed to investigate the effect of pH-mediated surface properties of bovine serum albumin (BSA) on protein aggregation and the changes of protein structure and colloidal stability at different solution pH levels. The hydrophobicity of BSA surface was characterized by endogenous fluorescence spectroscopy, fluorescence quenching of acrylamide, and fluorescence probe. The results showed that the hydrophobicity of BSA surface was similar at pH5, 6, 7.4, followed by pH4, 8, 9, 10, and finally by pH3 and 11 with strong acidity and alkalinity. The positive charge on the BSA surface was increased gradually with the decrease of solution pH, while the negative charge on protein surface was increased gradually with the increase of solution pH. The degree of protein aggregation was examined by turbidimetry, flow cytometry, and SDS-PAGE. The results showed that the oscillating aggregation of BSA did not change with the solution pH, but was partially dependent on the relative contribution of electrostatic and hydrophobic interactions between the protein molecules. In addition, the secondary structure, conformational stability, unfolding degree, and colloidal stability of proteins were investigated by circular dichroism, fluorescence spectroscopy, protein pulse hydrolysis, and dynamic light scattering, respectively. The results suggested that the solution pH could change the structure and stability of the protein at different levels. Solution pH has distinct effects on the structural stability of protein at different levels. The change of protein surface properties mediated by solution pH is related to protein aggregation.

Preparation of BSA surface imprinted manganese dioxide-loaded tubular carbon fibers with excellent specific rebinding to target protein

Along with the wide development of protein imprinted polymers, the researchers still face many challenges, such as difficult template elution, slow adsorption rate and low adsorption capacity. In order to promote the progress of protein separation and purification, the surface imprinted manganese dioxide-loaded tubular carbon fibers (FTCFs@MnO2@MIPs) are prepared in this work. FTCFs@MnO2@MIPs are based on tubular carbon fibers (TCFs) coated with flaky MnO2. Dopamine (DA) and bovine serum albumin (BSA) are utilized as functional monomers and templates. The MnO2 nanosheets are grown and loaded on the surface of carboxyl-modified tubular carbon fibers (CMTCFs) to form a MnO2 shell, which provides more imprinting sites for protein imprinting. Meanwhile, this shell enhances the interaction between the imprinting sites and BSA. The content of MnO2 loaded on the surface of CMTCFs is 9.42%. The obtained materials are systematically characterized and the adsorption performances of FTCFs@MnO2@MIPs for BSA are investigated. The adsorption process of FTCFs@MnO2@MIPs exhibits significant self-driven characteristics. The adsorption capacity reaches 816.44 mg/g in 60 min and the imprinting factor (IF) is 3.31. FTCFs@MnO2@MIPs can selectively separate BSA from the mixed proteins and fetal bovine serum. Excellent reusability and practical application ability make MnO2-loaded tubular carbon fibers (FTCFs@MnO2) become a promising carrier in the field of protein imprinting.

Mimicking biological process to detect alkaline phosphatase activity using the vitamin B6 cofactor conjugated bovine serum albumin capped CdS quantum dots

This manuscript presents a novel bioanalytical approach for the selective ratiometric fluorescent sensing of enzymatic activity of the alkaline phosphatase (ALP) in the biological samples. The probe was designed by conjugating the pyridoxal 5′-phosphate (PLP) over the surface of bovine serum albumin (BSA) stabilized CdS quantum dots (QDs) through the interaction of free amine present in BSA with the aldehyde group of PLP. The conjugation of PLP quenched the emission of QDs. Upon addition of the ALP, the emission of QDs was restored due to the dephosphorylation and the conversion of the functionalized PLP in to pyridoxal. With this probe, the ALP activity can be detected down to 0.05 U/L and also successfully applied for the detection of ALP activity in biological samples such as human serum and plasma.

The study of the interaction mechanism between bovine serum albumin and single-walled carbon nanotubes depending on their diameter and concentration in solid nanocomposites by vibrational spectroscopy.

The results of the study of composites based on bovine serum albumin (BSA) and single-walled carbon nanotubes (SWCNT) are presented. Nanocomposites were created by evaporation of the water-albumin dispersion with nanotubes using diode laser with temperature control. Two types of nanotubes were used. SWCNT I were synthesized using the electric arc method, SWCNT II were synthesized using the gas phase method. SWCNT I had a diameter and length less than SWCNT II. The mechanism of interaction between BSA and SWCNT in solid nanocomposites is considered. An experimental and theoretical studies of the interaction between aspartic (Asp) and glutamic (Glu) amino acids located on the outer surface of BSA and nanotubes using of vibrational spectroscopy (Fourier-transform infrared (FTIR) and Raman spectroscopy) was carried out. The possibility of nanotubes functionalization by oxygen atoms of negative amino acid residues Asp and Glu, which are on the outer surface of BSA, is shown by molecular modeling. The formation of covalent bonds between BSA and SWCNT in nanocomposites with different concentrations of nanotubes (0.01, 0.1 and 1 g/l) was confirmed by vibrational spectra. The covalent interaction between BSA with SWCNT under the laser irradiation leads to the conformational changes in the secondary and tertiary structures of albumin. This is confirmed by a significant decrease in the intensity of the absorption bands in the high-frequency region. The calculation of the vibrational spectra of the three Glycine:Glycine, Glutamic acid:Threonine and Aspartic acid:Lysine complexes, which take into account hydrogen, ion-dipole and ion-ion bonds, showed that a disturbance in the intermolecular interaction between amino acid residues led to significant decrease in the intensity of absorption bands in the region of stretching vibrations bonds OH and NH. From the Raman spectra, it was found that a significant number of defects in SWCNT is caused by the covalent attachment of oxygen atoms to the graphene surface of nanotubes. An increase in the diameter of nanotubes (4 nm) has practically no effect on the absorption spectrum of nanocomposite, while measuring the concentration of SWCNT affects the FTIR spectra. This confirmed the hydrophobic interaction between BSA and SWCNT. Thus, it was shown that BSA solid nanocomposites with CNTs can interact either with the help of hydrophobic forces or with the formation of covalent bonds, which depends on the diameter of the used nanotubes. The viability of connective fibroblast tissue cells on nanocomposites with both types of SWCNT was demonstrated. It was found that nanocomposites based on SWCNT I provide slightly better compatibility of their structure with fibroblasts. It allows to achieve better cell adhesion to the nanocomposite surface. These criteria make extensive use of scaffold nanocomposites in biomedicine, depending on the requirements for their quality and application.