Interaction Of Bovine Serum Albumin Research Articles

Interaction of 4-ethyl phenyl sulfate with bovine serum albumin: Experimental and molecular docking studies.

4-ethyl phenyl sulfate (EPS), a protein-bound uremic toxin found in serum of patients suffering from autism spectrum disorders (ASD) and chronic kidney disease (CKD). As per recent advances in the field, gut metabolites after their formation goes to blood stream crosses blood brain barrier and causes neuro related problems. Increased levels of 4-EPS in human body causes anxiety in patients and its role remains elusive. 4-EPS interacts with serum albumin in human body and thus, a model study of interaction of BSA with 4-EPS is presented in support of it. Absorption spectroscopy result demonstrated decrease in bovine serum albumin (BSA) absorption upon interaction with increasing concentration of EPS in a range from 2 μM to 100 μM. Moreover, this interaction was confirmed by the fluorescence quenching in presence of metabolite. The change in secondary structure was demonstrated by circular dichroism, synchronous fluorescence and Fourier transform infra-red spectroscopy. Docking studies reveals binding score of -5.28 Kcal mol-1, demarking that 4-EPS is involved in interaction with BSA via amino acid residues, forming the stable complex. This interaction study may be helpful in devising strategies for the treatment of chronic kidney disease and other neuro related diseases, by producing synthetic compound that competes with albumin binding sites to allow 4-EPS clearance from the body.

Tissue-Adaptive BSA Hydrogel with Dual Release of PTX and bFGF Promotes Spinal Cord Injury Repair via Glial Scar Inhibition and Axon Regeneration.

Spinal cord injury (SCI) is a severe clinical disease usually accompanied by activated glial scar, neuronal axon rupture, and disabled motor function. To mimic the microenvironment of the SCI injury site, a hydrogel system with a comparable mechanical property to the spinal cord is desirable. Therefore, a novel elastic bovine serum albumin (BSA) hydrogel is fabricated with excellent adhesive, injectable, and biocompatible properties. The hydrogel is used to deliver paclitaxel (PTX) together with basic fibroblast growth factor (bFGF) to inhibit glial scar formation as well as promote axon regeneration and motor function for SCI repair. Due to the specific interaction of BSA with both drugs, bFGF, and PTX can be controllably released from the hydrogel system to achieve an effective concentration at the wound site during the SCI regeneration process. Moreover, benefiting from the combination of PTX and bFGF, this bFGF/PTX@BSA system significantly aided axon repair by promoting the elongation of axons across the glial scar with reduced reactive astrocyte secretion. In addition, remarkable anti-apoptosis of nerve cells is evident with the bFGF/PTX@BSA system. Subsequently, this multi-functionalized drug system significantly improved the motor function of the rats after SCI. These results reveal that bFGF/PTX@BSA is an ideal functionalized material for nerve repair in SCI.

Evaluation of protein-polysaccharide interactions through ζ-potential and particle size measurements to assess their functionality in wine.

Protein-polysaccharide-tannin interactions are important in every aspect of red wine production from physical stability to color, astringency, and body. For this model study, bovine serum albumin (BSA) was selected as the protein, while carboxymethyl cellulose (CMC), mannoproteins, and pectin were the model polysaccharides. Each protein-polysaccharide combination was analyzed for zeta (ζ) potential and particle size at neutral pH and within the wine-like solution. Mixtures were assessed regarding their protective, affinitive, and aggregative behaviors. Based on their individual ζ-potentials, pectin and mannoprotein were most stable at lower concentrations. At higher concentrations, they reduced the suspension's stability and increased the aggregate sizes. CMC consistently increased the stability of any solution under neutral pH conditions. However, with increasing concentrations, these large aggregates are expected to precipitate. Fruit pectin (FP) and BSA interactions seemed to be the main factors in the formation of visible precipitates at neutral pH. FP and the mannoprotein decreased stability enough to cause precipitation without haze formation. The mannoprotein decreased particle sizes, in both the suspension and precipitation, which may indicate greater selectivity toward proteins. FP also decreased the suspended particle sizes under wine conditions. These findings demonstrate the use of ζ-potential and particle size values to characterize macromolecular interactions in model systems and can also be used to indicate effective fining agents. PRACTICAL APPLICATION: This work demonstrates the capabilities of ζ-potential analysis paired with size particle measurements to predict and characterize the interactions between macromolecules in complex systems. The interactions between model wine macromolecules can be evaluated with this technology at a level that cannot be reached with any other analytical technique.

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.

Synthesis of tetranuclear cyclopalladated complex using thiosemicarbazone derivative ligand: Spectral, biological and molecular docking studies

New tetranuclear Palladium(II) complex, (Pd-(OMe)-TSC)4, has been successfully synthesized from the reaction of potassium tetrachloridopalladate (II) salt (K2[PdCl4]) with methoxy‑functionalized thiosemicarbazone ligand, OMe-TSC, and characterized using various spectroscopic techniques such as FT-IR, UV–Vis, 1H NMR, 13C NMR, 1H-1H COSY, 13C-APT, 1H-13C HMQC, elemental analyses and high-resolution mass spectroscopy. The in-vitro anticancer activity was investigated by using MTT test in breast cancer cells (MCF-7 cell line). Anticancer activity of the complex was higher than ligand and the results inferred that the complex showed comparable activitiy with cis-platin. Furthermore, fluorescence and UV–Vis spectroscopies had been used to investigate the binding interaction of the synthesized samples with Bovine Serum Albumin (BSA). Three different drugs namely, Warfarin, Ibuprofen, and Digoxin, were employed to study the competitive bindings to different sites on BSA. The obtained results demonstrated that the binding sites were mainly located within site I and II of BSA for the (Pd-(OMe)-TSC)4 complex and (OMe)-TSC ligand, respectively. In addition, the suggested structures of ligand and complex have been optimized by semi-emprical method and the aforementioned results of BSA interaction were supported by molecular docking and molecular dynamics calculations. Also, The free binding energies of -4.16 kcal/mol and -5.80 kcal/mol were calculated for the interaction of the ligand and complex with SARS-CoV-2, respectively, which indicated the interaction is a spontaneous process and is a evidence for antiviral potential of (Pd-(OMe)-TSC)4 complex.

Dynamic spectroscopic and optical characterization and modeling of bovine serum albumin corona during interaction with N-hydroxysulfo-succinimide-covalently functionalized gold nanourchins.

In this study, bovine serum albumin (BSA) is used as a globular protein model to examine the conformational changes that occur during the interaction of BSA with N-hydroxysulfo-succinimide (sodium salt)-functionalized gold nanourchins (GNUs), for which dynamic spectroscopic techniques are employed. The results showed that the absorbance of phosphate-buffered saline-BSA at 278 nm decreased when a GNU was added to the solution due to adsorption, and it decreased further when the GNU was increased. The intensity and width of the peak of local surface plasmon resonance increased, indicating the effect of corona formation. Dynamic UV-vis spectroscopy and scattering revealed a nonlinear behavior of BSA-GNU interaction. The bioplasmonic solution resulted in higher transmission and scattering than the BSA solution. Fourier transform-near-infrared spectra exhibited several bands due to overtones and combinations of the amide group and different proportions of α-helix and β-sheet components in BSA before and after the addition of the GNU. Time-resolved fluorescence spectroscopy demonstrated an initial increase in blueshifted emission, followed by a redshifted quenching of two major peaks of Tyr and tryptophan (Trp). The binding and dissociation constants were determined as Kb = 2.17 × 1010 M-1 and Kd = 4.6 × 10-11, respectively, using the Stern-Volmer relation. Both the dynamic CMOS-based imaging and the cadmium sulfide sensors demonstrated a nonlinear response of bioplasmonic solution. By increasing the GNU, the resistance of the solution decreased in the order of A > S1 > S3, where S3 exhibited the highest initial transmission with a longer desorption time. MATLAB modeling showed 80% surface coverage by the protein in 15 s at 0.05M, equivalent to a thickness of 1.7 nm, which was in agreement with the value determined by using the Stokes-Einstein relation.

2-Propyl-1H-imidazole-4,5-dicarboxylate acid supported cu/ni/fe/co complexes: synthesis, biological and catalytic evaluation

Herein, we report 2-propyl-1H-imidazole-4,5-dicarboxylate complexes of Cu/Co/Fe/Ni metal ions. The complexes have been characterized using powder X-ray diffraction, FTIR, and mass spectrometry. Thermal gravimetric analysis (TGA) established their thermal stability, enduring temperatures of up to 650 °C. The interaction of Bovine Serum Albumin (BSA) and DNA with these complexes was examined, revealing a significant binding affinity up to 70%. Fluorescence quenching experiments also showed the binding of complexes with biomolecules. These interactions were substantiated by molecular docking studies against the proteins 3v03 (BSA) and 1d28 (DNA), shedding light on the essential interactions driving their potential medicinal activity. The Cu complex displayed a notably high GSC score and a substantial area as determined through the Patch Dock server. Free radical interaction with 2,2-diphenylpicrylhydrazyl (DPPH) shows their antioxidant activity where Cu and Fe complexes expressed greater activity as compared to others. The catalytic properties of the compounds were assessed using p-nitrophenol (PNP) where the complexes exhibited reducing activity, leading to a conversion of over 90% of PNP into p-aminophenol. Analysis revealed a pseudo-second-order model closely aligned with experimental values, indicating second-order reduction kinetics.

Development of theaflavins-loaded albumin nanoparticles and in silico analysis of theaflavins: BSA interaction

Theaflavins (TFs), bioactive compounds present in black tea manufactured from Camellia sinensis leaves have potential health benefits. Due to their instability and low bioavailability, we have encapsulated TFs into albumin nanoparticles (Alb-TFs-NP) and characterized them using different techniques. The mean particle size of Alb-TFs-NP was 125.9 nm with a low (0.23) polydispersity index and Zeta potential of -76.8 mV. Scanning electron microscopy (SEM) and Transmission electron microscopy (TEM) analysis revealed a spherical shape of Alb-TFs-NP with a smooth surface. The fluorescence of bovine serum albumin (BSA) and TFs was at 280 nm and 660 nm excitation and 690-700 nm emission respectively. The BSA-TFs complex interacts at distinct amino acid binding sites with good docking energy of TF1 (-10.5 kcal/mol-1), TF2 (-11.1 kcal/mol-1), TF2a (-11.2 kcal/mol-1) and TF3 (-10.4 kcal/mol-1) at the BSA active site. Primarily hydrogen bonding was involved in the BSA-TFs interaction. The study could further research the transport distribution and bioactivities of TFs in the human body.

Mathematical modelling of genipin-bovine serum albumin interaction using fluorescence intensity measurements

The interaction between genipin and a model protein bovine serum albumin (BSA), with and without the addition of acetic acid, has been studied experimentally and by modelling. The number of amino groups available to react was determined to be 5.6 % of the total number of amino acid building blocks on BSA. Fluorescence intensity was used to record the progress of the reaction over the 24 h, while the modelling study focused on capturing the kinetic profiles of the reaction. The experiments revealed a slow start to the BSA and genipin interaction, that subsequently accelerated in an S-shaped curve which the modelling study linked with the existence of the feedback cycle for both reactive amino groups and genipin. At BSA concentrations ≥30 mg/mL the reaction was accelerated in the presence of acid, while below 30 mg/mL the acidified conditions delayed the onset of the reaction. Contrary to the reaction mechanisms previously proposed, a degree of breakdown of the fluorescent links in the products formed was denoted both experimentally and in a modelling study. This indicated the reversibility of the processes forming fluorescent product/s and suggested feasibility of the successful release of the protein following prospective encapsulation within the genipin-crosslinked hydrogel structure.

Exploring albumin-sulfonephthalein dyes interactions by a chemometric-assisted and multi-technique equilibria analysis in solution

Albumin is undoubtedly the most studied protein thanks to its widespread diffusion and biochemistry; despite its binding ability towards different dyes, provoking dye’s colour change, has been exploited for decades for quantification purposes, the joint effect of working pH, ionic strength, and dye’s pKa still remains only sporadically discussed. In the present study, the interaction of Bovine Serum Albumin (BSA) with five dyes belonging to the sulfonephthalein group, Bromophenol Blue (BPB, pKa = 3.75), Bromocresol Green (BCG, pKa = 4.42), Chlorophenol Red (CPR, pKa = 5.74), Bromocresol Purple (BCP, pKa = 6.05) and Bromothymol Blue (BTB, pKa = 6.72), is investigated at four working pH values (3.5, 6.0, 7.5 and 9.0) and two ionic strength conditions by UV–Vis spectroscopy. Principal Component Analysis is then applied to rationalize dye behavior upon BSA addition at each pH value and to summarize the protein effect on dyes’ spectral features, identifying three general behaviors. The most relevant systems are then submitted to further characterization involving a solution equilibria study aimed at determining conditional binding constants for the selected DSA-dye adducts and fluorescence, CD, and 1H NMR spectroscopy to evaluate the binding effect on the species involved.

Effect of irradiated nonionic surfactant on drug-protein binding

In this work, the effect of γ-irradiated surfactants on drug–protein binding has been assessed. Irradiated aqueous solutions of Pluronic F-127, Pluronic L-35, Tween 20, and Tween 80 surfactants were used. Gamma irradiation was carried out for three different doses, to these four surfactants viz., 6, 30, and 36 kGy. Two drugs, Ornidazole (ONZ) and Telmisartan (TMS) were used for the binding study. The effect of four irradiated surfactants in the presence of drug – Bovine serum albumin (BSA) protein was analyzed. The drug solutions in methanol-aqueous media were combined with BSA in the initial step. In the next two succeeding steps, drug–BSA interaction in the presence of unirradiated and irradiated surfactants were carried out. The results of drug-BSA due to addition of irradiated and unirradiated surfactants were compared. The interaction processes were assessed through UV Spectroscopy, DLS, zeta potential, turbidity, and docking studies. Improved binding was observed for both the drugs and four surfactants for irradiated surfactants as determined from the binding constant values using UV spectroscopic studies. The DLS measurements demonstrated no general trend of increase or decrease in micellar size with absorbed dose. The binding and change in the size of micelles were observed to be highly drug and surfactant-specific. Among the four surfactants, irradiated Pluronic F-127 showed higher binding affinity. To the best of our knowledge, this is the first report on the effect of γ-irradiated surfactant on drug–BSA interaction. This can be applied to other drug–protein systems to tune their interaction to the required level. Communicated by Ramaswamy H. Sarma

Unveiling the antimicrobial potency and binding interaction between sulfonamide substituted Schiff’s bases and BSA protein: An integrated experimental and theoretical approach

Sulfonamide derived Schiff’s bases encompass significant properties such as antifungal, anti-inflammatory, anticancer, antibacterial, antiproliferative, and antioxidant and hold a central position in therapeutics and diagnostics. Hence, it is essential to comprehend their interconnection with carrier proteins such as Bovine serum albumin (BSA). Herein, two different sulfonamide derived Schiff’s base derivatives,N'-(2,5-Dimethoxybenzylidene)-4-methylbenzenesulfonohydrazide SB-1 and N'-(3-Bromo-4-methoxybenzylidene)-4-methylbenzenesulfonohydrazide SB-2 were synthesized by reacting respectivealdehydes with p-toluenesulfonyl hydrazide as the amine counterpart in absolute ethanol and structurally characterized by FT-IR,1H and13C NMR, elemental analyses, thermogravimetric analysis (TGA), mass spectrometry and single-crystal X-ray crystallography. The binding interactions between BSA andSB-1 and SB-2were made by employing UV–vis. absorption and fluorescence spectroscopy. Information about the binding constant was obtained from the absorbance enhancement and fluorescence quenching of BSA in the presence ofSB-1 and SB-2respectively. However, the binding efficiency ofSB-1was found to be superior to that of BSA in comparison toSB-2. The antibacterial potential ofSB-1 and SB-2 wastested on E. coliandS. aureus using thewell diffusion method.In silicoADME properties forSB-1 and SB-2were checked to assess their stability. The binding mechanisms to the specific enzymes associated with the BSA interaction and the antibacterial capabilities of theSB-1 and SB-2were further supported by molecular docking calculations. The detailed studies provide comprehensive data to support the utility of prepared Schiff’s bases as potential biomarkers in therapeutics.

Clarifying the role of carboxyl functionality in squaraines towards aggregation and self-assembly through photophysical characterization and BSA interactions

The demand for near-infrared (NIR) probes with robust and stable fluorescence signals has surged, driven by their applications in optical sensing and bioimaging. Squraine dyes as NIR fluorescent probes have gained significant traction. However, understanding their behavior in aqueous media is important for their successful application. Herein we report the synthesis and photophysical characterization of carboxy-functionalized unsymmetrical squaraine dyes capable of light absorption and emission in the near-infrared (NIR) wavelength region. Structural variations in alkyl chain length, and spacer chain length between the primary chromophore and –COOH group were systematically introduced to investigate their impact on self-assembly in aqueous media leading to dye aggregation and their differential interactions with Bovine Serum Albumin (BSA) as a model protein. In phosphate buffer (PB) the absorption intensity decreased drastically along with pronounced shoulders due to dye aggregation leading to complete fluorescence quenching. However, in the presence of BSA, the intensity of shoulder bands reduced coupled with a sharp increase in the absorption associated with monomeric dye with the increasing concentration of BSA, indicating the prevention of dye aggregation owing to dye-BSA interactions. The prevention of dye aggregation due to dye-BSA interaction also led to a tremendous increase in the fluorescence intensities as a function of the increasing BSA concentrations. Site-selective study off BSA showed that these dyes bind preferably at Site-II using hydrophilic interactions. Thus, these dyes show great potential as FRET or fluorescent on/off probes for biosensing, non-covalent labeling of proteins, and fluorescent probes for bioimaging.

Synthesis, characterization, and BSA binding studies of newfangled 2-phenylacetohydrazide derivatives

Five 2-phenylacetohydrazide derivatives (BPAH = N′-benzylidene-2-phenylacetohydrazide, HBPAH = N’-(2-hydroxybenzylidene)-2-phenylacetohydrazide), PPAH = 2-phenyl-N′-3-phenylallylideneacetohydrazide, FMPAH = N’-(furan-2-ylmethylene)-2-phenylaceto hydrazide and EPAH = N′-ethylidene-2-phenylacetohydrazide were synthesized by the condensation of 2-phenylacetohydrazide with the corresponding aldehyde. The synthesized compounds were characterized by FTIR, 1D, and 2D NMR spectroscopy. The structure of the BPAH and PPAH were analyzed by single crystal X-ray diffraction analysis and in both crystallized compounds, the molecules adopted trans geometry around the –CN- (imine) functional group. To explore the pharmacological significance of these compounds, the binding ability of these compounds with Bovine Serum Albumin (BSA) was investigated using fluorescence spectroscopy. BPAH and PPAH showed the highest binding ability while EPAH, HBPAH, and FMPAH had lower binding ability to BSA molecules. Thermodynamic parameters ΔG, ΔH°, and ΔS° demonstrated that interactions of BSA with compounds BPAH, EPAH, FMAH, and HBPAH were exothermic while for PPAH it was endothermic. The negative enthalpy and entropy of the compounds BPAH, EPAH, FMAH, and HBPAH indicated that van der Waals' forces and hydrogen bonding played a major role in stabilizing the BSA binding with the molecules. Hydrophobic interactions were predominant in the binding of PPAH with BSA tends to interact with two sets of BSA binding sites with an increase in temperature.

Investigating the binding interaction of quinoline yellow with bovine serum albumin and anti-amyloidogenic behavior of ferulic acid on QY-induced BSA fibrils

Protein aggregation induces profound changes in the structure along with the conformation of the protein, and is responsible for the pathogenesis of a number of neurodegenerative conditions such as Huntington’s, Creutzfeldt–Jacob, Type II diabetes mellitus, Alzheimer’s, etc. Numerous multi-spectroscopic approaches and in-silico experiments were utilized to investigate BSA’s biomolecular interaction and aggregation in the presence of quinoline yellow. The present research investigation evaluated the interaction of BSA with the food colorant (QY) at two different pH (7.4 and 2.0). The development of the BSA-QY complex was established with UV visible and fluorescence spectroscopy. The quenching of fluorescence upon the interaction of BSA with QY revealed the static nature of quenching mechanism. The Kb value obtained from our result is 4. 54 × 10−4 M−1. The results from the competitive site marker study infer that quinoline yellow is binding with the sub-domain IB of bovine serum albumin, specifically on site III. Three-dimensional fluorescence and synchronous fluorescence spectroscopy were applied for monitoring the alterations in the microenvironment of BSA upon the addition of quinoline yellow. The results from turbidity and RLS studies showed that higher concentrations of QY (80–400 µM) triggered bovine serum albumin (BSA) aggregation at pH 2.0. At pH 7.4, QY couldn’t manage to trigger bovine serum albumin aggregation, perhaps because of the repulsion between negatively charged dye (QY) and anionic bovine serum albumin. The results from far-UV CD, Congo Red, and scanning electron microscopy implicate that the QY-induced aggregates exhibit amyloid fibril-like structures. Molecular docking results revealed that hydrophobic interactions, hydrogen bonding, and Pi-Sulfur interactions contribute to QY-induced aggregation of BSA. Further, the amyloid inhibitory potential of ferulic acid (FA), a phenolic acid on QY-induced aggregation of BSA, has also been assessed. The QY-induced amyloid fibrils are FA-soluble, as confirmed by turbidity, RLS, and far-UV CD studies. Far-UV CD results showed that FA retains α helix and inhibits cross β sheet formation when the BSA samples were pre-incubated with increasing concentrations of FA (0–500 µM). Our findings conclude that QY dye successfully stimulates BSA aggregation, but ferulic acid inhibits QY-induced aggregation of BSA. Thus, FA can serve as a therapeutic agent and can help in the treatment of various amyloid-related conditions.

Biophysical insight into the binding mechanism of 1,3-benzodioxole-based lidocaine tagged ionic liquids with BSA: An in-silico, and spectroscopic studies

The interaction between bio-macromolecules and drugs has attracted significant interest for several decades due to their pharmacokinetics and pharmacological implications. Ionic liquids have a major importance in the development of effective drugs that can majorly target and bind to the proteins present in the body. A slight disturbance in the micro-environment of protein induced by a drug can alter the conformations of proteins to lead them to work differently. The interaction of ionic liquids with proteins present in blood such as HSA (Human Serum Albumin) and BSA (Bovine Serum Albumin) provides useful evidence for synthesizing API-based liquid drug and their delivery. In this study, the interaction of BSA with LPAc & LPOT ILs (LPAc: N-(benzo[d][1,3]dioxol-5-ylmethyl)-2-((2,6-dimethylphenyl)amino)-N,N-diethyl-2-oxoethan-1-aminium acetate and LPOT: N-(benzo[d][1,3]dioxol-5-ylmethyl)-2-((2,6-dimethylphenyl)amino)-N,N-diethyl-2-oxoethan-1-aminiumtrifluoromethane sulfonate) using spectroscopic methods like UV–visible, fluorescence, CD spectroscopy, computational studies (molecular docking, MD simulation studies, and ADMET studies). UV–vis spectra showed a slight rise in absorbance intensity with the addition of ionic liquid. A static quenching of BSA with blue shift was observed according to fluorescence spectra on the addition of ionic liquids (LPAc & LPOT) and conformational alterations of BSA were observed by analyzing CD spectra. LPAc and LPOT showed strong binding with BSA with molecular docking scores of −330.2 and −365.2 kcal/mol respectively. The molecular dynamic simulation and in-silico pharmacological and pharmacokinetics studies support the spectroscopic study and molecular docking results inferring that LPOT ionic liquid showed strong binding interactions with BSA. In-vitro studies against A549 cell lines showed that both LAPc and LPOT ionic liquids had antiproliferative properties and LPOT has better anticancer activity as inferred by IC50 value: 38.83 and may be further useful for drug design as cancer therapeutic.

Exploration of the intermolecular isoproturon–bovine serum albumin combination: Biophysical and computational prospects

Isoproturon (IPU), a selective systemic herbicide that is frequently applied to eradicate large-leaved weeds and annual grasses in agricultural fields. However, the accumulation of IPU residues during food production might negatively affect on human and animal health. To comprehend the impact of IPU on the mankind and environment, the interaction analysis of IPU with plasma protein is crucial. This work used a variety of techniques, including fluorescence, UV–vis absorption, computational docking and dynamics simulation to extensively examine the combination of IPU with bovine serum albumin (BSA) under typical physiological settings. IPU quenched the BSA fluorescence and form the IPU–BSA complex through a static process. A weak binding affinity was anticipated (binding constant = 4.68–2.48 × 103 M−1) for IPU–BSA interaction. Thermodynamic results revealed that the IPU–BSA binding reaction was a spontaneous process, predominantly governed by hydrogen bonds, van der Waals and hydrophobic forces, which was well supported by molecular docking analysis. Synchronous and three-dimensional fluorescence spectral results exhibited microenvironmental fluctuations near the protein’s Trp and Tyr residues with added IPU, but inclusion of IPU to BSA was observed to enhance the protein’s thermal constancy. Site marker displacement results demonstrated that IPU desirably binds to BSA at site II. An in silico findings also unveiled the primary binding arrangement of IPU was placed at site II of BSA and surrounded by hydrophobic and polar residues. Molecular dynamics simulation results suggested the IPU–BSA complex persisted compact and stable.

Synthesis of an Aryl-Semicarbazone-Based Cu(II) Complex for DNA and BSA Interaction and Anti-Cancer Activity against Human Cervix Uteri Carcinoma

The current study provides an in-depth analysis of the biological properties of a Cu(II) complex (C22H24Cu2N6O10) obtained from an aryl-semicarbazone ligand derived (L) from the condensation of 2,4-dihydroxy acetophenone and semicarbazide. The binding behavior of this complex with calf thymus DNA (CT-DNA) and bovine serum albumin (BSA) protein was explored using a combination of experimental and theoretical approaches. The results suggest that the complex binds with CT-DNA via a partial intercalation, and hydrophobic interaction. However, the complex binds to BSA protein predominantly through hydrogen bonding or van der Waals interactions rather than hydrophobic interactions. The molecular docking methodology was carried out to substantiate the experimental finding. Furthermore, the in vitro cytotoxicity study was conducted on human cervix uteri carcinoma (SiHa cancerous cell) lines upon exposure to the complex, and the findings reveal a considerable decrease in cell viability, when compared to the control. Overall, this study provides a comprehensive understanding of the biological potential of the Cu(II) complex and its potential as an anti-cancer agent.

Probing the biomolecular interactions of oxidized Ti3C2Tx nanosheets: How surface chemistry influences serum protein binding

Ti3C2Tx has promising applications in the biomedical field due to its biocompatibility, hydrophilicity, and antibacterial activity. However, its effects on health are still being explored. This study analyzes the interaction of bovine serum albumin (BSA) with Ti3C2Tx at different levels of oxidation. Zeta potential measurements showed that the colloidal stability of Ti3C2Tx varied with the degree of oxidation, with unoxidized Ti3C2Tx (U-Ti3C2Tx) being the most stable, followed by fully oxidized Ti3C2Tx (F-Ti3C2Tx) and partially oxidized Ti3C2Tx (P-Ti3C2Tx). UV–Vis absorption and fluorescence spectroscopy confirmed that the formation of Ti3C2Tx-BSA complexes resulted in fluorescence quenching. In addition, synchronous fluorescence spectroscopy, Fourier transform infrared spectroscopy and circular dichroism showed that the interaction between F-Ti3C2Tx and BSA altered the secondary conformation of BSA, and that U-Ti3C2Tx had a weaker effect on the conformation of BSA. Molecular docking results emphasized that hydrogen bonding is the main driving force between Ti3C2Tx and BSA.

The effect of fatty acids, ionic strength, and electric fields on the microscopic dynamics of BSA aggregates

This paper presents the microscopic dynamics of the concentrated suspensions of bovine serum albumin (BSA) proteins and their aggregates by dynamic light scattering (DLS) experiments. The effects of fatty acids binding to BSA, as well as the ionic strength and weak electric field, are discussed for affecting the stability of BSA suspensions against calcium-induced aggregation. By variation of the ionic strength, in the absence of an external electric field, DLS experiments show that monomer–BSA interactions (in the essentially fatty acid-free case) are overall repulsive but that, nevertheless, aggregation occurs to some extent. Also, the diffusive properties of different types of BSA are explored under an applied low-AC electric field by means of in situ electric small-angle depolarized DLS experiments, which reveal a significant decrease of the translational BSA–monomer diffusion coefficient with increasing frequency, while the aggregates indicate orientational motion via rotation on applying an electric field. These observations are interpreted in terms of (localized) orientation interactions obtained as oscillations in the intermediate scattering correlation function, as well as the anomalous slower relaxations as resulting in effective (collective) dynamics between monomeric BSA and their protein aggregates.