Between Bovine Serum Albumin Research Articles

Unveiling Fluorescence Spectroscopy, Molecular Docking and Dynamic Simulations: Interactions Between Protein and 2, 4-Dinitrophenylhydrazine Schiff Base.

In this study, we aimed to explore the interaction mechanism between bovine serum albumin (BSA) and a Schiff base compound derived from 2,4-dinotrophenyl hydrazine (L) using various spectroscopic techniques. The interaction between BSA and synthesizing molecule can provide insights into binding affinity, conformational changes and potential applications in drug delivery or biochemistry. The interaction between BSA and L was studied by using UV-Vis and fluorescence titration analysis. The fluorescence quenching emission was observed at 343nm, upon addition of L to the buffer solution of BSA. The binding between BSA and ligand is static in nature using fluorescence quenching emission. The thermodynamic parameters were calculated from the temperature-dependent binding constants (i.e., ∆H = -0.318kcal/mol, ∆G = -7.857kcal/mol and ∆S = 0.023kcal/mol), which indicated that the protein-ligand complex formation between L and BSA is mainly due to the electrostatic interactions. The experimental and theoretical results showed excellent agreement with respect to the mechanism of binding and binding constants. The molecular docking and molecular dynamic analysis experiments were performed to establish the interaction between protein and ligand.

Green synthesis of zinc ferrite nanoparticles from Nyctanthes arbor-tristis: unveiling larvicidal potential, protein binding affinity and photocatalytic activities.

Environmental pollution, being a major concern worldwide, needs a unique and ecofriendly solution. To answer this, researchers are aiming in utilizing plant extracts for the synthesis of nanoparticles. These NPs synthesized using plant extracts provide a potential, environmentally benign technique for biological and photocatalytic applications. Especially, plant leaf extracts have been safe, inexpensive, and eco-friendly materials for the production of nanoparticles in a greener way. In this work, zinc ferrite nanoparticles (ZnFe2O4 NPs) were prepared using Nyctanthes arbor-tristis leaf extract by hydrothermal method, and its biological and photocatalytic properties were assessed. The synthesized ZnFe2O4 NPs were characterized using powder X-ray diffraction (XRD), scanning electron microscopy (SEM), and Fourier-transform infrared spectroscopy (FT-IR). X-ray diffraction confirmed the arrangement of the fcc crystal structure of the nanoparticles and that some organic substances were encapsulated within the zinc ferrite. According to the SEM analysis, the resulting nanoparticles got agglomerated and spherical in shape. The ZnFe2O4 nanoparticles are in their pure form, and all of their elemental compositions were shown by the energy-dispersive X-ray analysis (EDAX) spectrum. The FTIR results revealed that the produced nanoparticles contained distinctive functional groups. Fluorescence spectroscopy was used to examine the binding affinities between bovine serum albumin (BSA) and ZnFe2O4 nanoparticles in terms of protein binding, stability, and conformation. The interaction between BSA and ZnFe2O4 NPs was examined using steady-state and time-resolved fluorescence measurements, and it was evident that static quenching occurred. The ability of ZnFe2O4 nanoparticles to kill Culex quinquefasciatus (C. quinquefasciatus) larvae was evaluated. The synthesized NPs demonstrated a noteworthy toxic effect against the fourth instar larvae of C. quinquefasciatus with LC50 values of 43.529µg/mL and LC90 values of 276.867µg/mL. This study revealed the toxicity of green synthesized ZnFe2O4 NPs on mosquito larvae, proving that these NPs are good and effective larvicides. Furthermore, the ZnFe2O4 NPs were utilized for dye degradation of methylene blue under visible light treatment and achieved 99.5% degradation.

Exploring the binding characteristics of bovine serum albumin with CDK4/6 inhibitors Ribociclib: Multi-spectral analysis and molecular simulation studies

Ribociclib (RIB), a tyrosine kinase inhibitor, exhibits promising antitumor efficacy and controlled toxicity in HR+/HER2- breast cancer patients, which is closely related to the binding with plasma proteins. This study utilized a combination of spectroscopic techniques including UV spectroscopy, fluorescence spectroscopy, and circular dichroism (CD) as well as molecular docking and molecular dynamic simulation to clarify the binding mechanism between bovine serum albumin (BSA) and RIB. The findings demonstrated that RIB produced a 1:1 stoichiometric complex with BSA, which quenched BSA's fluorescence in the manner of the static quenching mechanism. Site labelling experiments pinpointed Site III on BSA as the primary binding site for RIB, a finding validated by molecular docking. Van der Waals forces and hydrogen bonding interactions as key drivers in the formation of RIB-BSA complexes, a conclusion supported by molecular docking. Molecular simulation studies suggested that the insertion of RIB into the hydrophobic cavity (Site III) of BSA induced subtle conformational changes in the BSA protein, and CD measurements confirmed alterations in BSA secondary structure content. Synchronous and three-dimensional fluorescence spectroscopy further demonstrated that RIB decreased the hydrophobicity of the microenvironment surrounding tyrosine and tryptophan residues. These findings offer valuable insights into the pharmacokinetics and structural modifications of RIB.

Revealing the interaction mechanism between bovine serum albumin (BSA) and a fluorescent coumarin derivative: A multispectroscopic and in silico approach

The interaction of biomacromolecules with each other or with the ligands is essential for biological activity. In this context, the molecular recognition of bovine serum albumin (BSA) with 4-(Benzo[1,3]dioxol-5-yloxymethyl)-7-hydroxy-chromen-2-one (4BHC) is explored using multispectroscopic and computational techniques. UV–Vis spectroscopy helped in predicting the conformational variations in BSA. Using fluorescence spectroscopy, the quenching behaviour of the fluorophore upon interaction with the ligand is examined, which is found to be a static type of quenching; fluorescence lifetime studies further verify this. The binding constant is discovered to be in the range of 104 M−1, which indicates the moderate type of association that results in reversible binding, where the transport and release of ligands in the target tissue takes place. Fourier-transform infrared spectroscopy (FT-IR) measurements validate the secondary structure conformational changes of BSA after complexing with 4BHC. The thermodynamic factors obtained through temperature-dependent fluorescence studies suggest that the dominant kind of interaction force is hydrophobic in nature, and the interaction process is spontaneous. The alterations in the surrounding microenvironment of the binding site and conformational shifts in the structure of the protein are studied through 3D fluorescence and synchronous fluorescence studies. Molecular docking and molecular dynamics (MD) simulations agree with experimental results and explain the structural stability throughout the discussion. The outcomes might have possible applications in the field of pharmacodynamics and pharmacokinetics.

Spiropyran molecular aggregates implanted photo-responsive graphene oxide membrane with self-cleaning ability for enhanced water purification

Stimuli-responsive separation membranes with adjustable interfacial properties are highly desired for energy-efficient and sustainable water purification, owing to their exceptional antifouling capability and separation selectivity. However, the construction of highly efficient responsive membranes continues to present a substantial challenge. Herein, photo-responsive spiropyran (SP) molecular aggregates obtained via a "good-poor" solvent self-assembly strategy were implanted into lamellar graphene oxide (GO) membrane. The obtained GO/SP membrane with enriched water transport channels and enhanced hydrophilicity demonstrated superior water permeability (95.0 L h−1 m−2 bar−1). Benefiting from the reversible photoisomerization of SP molecules between the hydrophobic SP upon light irradiation and the hydrophilic zwitterionic merocyanine (MC) in dark conditions, the GO/SP membrane possessed captivating photo-response property verified by tunable water permeability and molecular rejection. Theoretical calculation revealed that the thermodynamic interface energy between bovine serum albumin (BSA) and membrane surface changed from attraction in dark conditions to repulsion under light conditions. Consequently, the water permeability of BSA-fouled membranes could recover to 96.2 % of its initial level after light irradiation, exhibiting fascinating photo-driven self-cleaning capability. The designed photo-responsive membrane with feasible membrane fouling control holds great promise for efficient water purification.

Elucidation of binding mechanisms of bovine serum albumin and 1-alkylsulfonates with different hydrophobic chain lengths

In this article, the binding interactions between bovine serum albumin (BSA) and three 1-alkylsulfonates, namely sodium 1-dodecanesulfonate, sodium 1-decanesulfonate, and sodium 1-octanesulfonate, have been thoroughly investigated. The study employed various experimental techniques such as isothermal titration calorimetry (ITC), steady-state fluorescence spectroscopy (SF), circular dichroism spectroscopy (CD), and molecular dynamics-based simulations. The objective was to understand the influence of the alkyl chain length of the investigated ligands on several aspects, including the strength of the interaction, the stoichiometry of the resulting complexes, the number of BSA binding sites, and the underlying mechanisms of binding. Notably, the study also demonstrated that sodium dodecyl sulfate (S12S) can serve as an effective site marker for BSA when studying ligands with similar structural and topological features. These findings may have significant implications for enhancing our understanding of the interactions between small amphiphilic molecules and proteins.

Interaction of eugenol-based anti-tuberculosis nanoemulsion with bovine serum albumin: A spectroscopic study including Rifampicin, Isoniazid, Pyrazinamide, and Ethambutol

Tuberculosis (TB), a deadly infectious disease, is primarily caused by the bacterium Mycobacterium tuberculosis. The misuse of antibiotics has led to the development of drug resistance, prompting researchers to explore new technologies to combat multidrug-resistant Tuberculosis (MDR TB). Phospholipid-based nanotherapeutics, such as nanoemulsions, are gaining traction as they enhance drug solubility, stability, and bioavailability. Our study focuses on the interaction between Bovine Serum Albumin (BSA) and a drug-loaded nanoemulsion based on Eugenol. This nanoemulsion incorporates Eugenol, Clove, cinnamon oil, and first-line anti-tuberculosis drugs like Rifampicin, Isoniazid, Pyrazinamide, and Ethambutol. The primary objective is to assess the biosafety profile of the nanoemulsion upon interaction with BSA. We employed Fluorescence, UV–visible, and Fourier Transform Infrared Spectroscopy (FTIR) to analyze this interaction.UV–visible spectroscopy detected changes in hydrophobicity due to structural alterations in BSA near the tryptophan residue, leading to the formation of ground-state complexes. Fluorescence spectroscopy demonstrated that the nanoemulsion effectively quenched fluorescence originating from tryptophan and tyrosine residues. Studies using synchronous and three-dimensional spectroscopy point to a potential modification of the aromatic environment of BSA by the nanoemulsion. Resonance light scattering spectra indicated the formation of large aggregates due to the interaction with the nanoemulsion. The second derivative FTIR spectra showed an increase in the magnitude of secondary structure bands, suggesting a conformational shift. This research has significant pharmacological implications for developing safer, more targeted drug delivery systems. The information obtained from the interaction of the nanoemulsion with the blood carrier protein is vital for the future development of superior carriers with minimal adverse effects on patients. It is crucial to remember that conformational changes brought on by drug-ligand complexes attaching to carrier proteins may have negative consequences. Therefore, this study enhances the in vitro evaluation of potential adverse effects of the nanoemulsion on serum proteins.

Design and characterization of BSA-mycophenolic acid nanocomplexes: Antiviral activity exploration

The interactions between bovine serum albumin (BSA) and mycophenolic acid (MPA) were investigated in silico through molecular docking and in vitro, using fluorescence spectroscopy. Dynamic light scattering and scanning electron microscopy were used to figure out the structure of MPA-Complex (MPA-C). The binding affinity between MPA and BSA was determined, yielding a Kd value of (12.0 ± 0.7) μM, and establishing a distance of 17 Å between the BSA and MPA molecules. The presence of MPA prompted protein aggregation, leading to the formation of MPA-C. The cytotoxicity of MPA-C and its ability to fight Junín virus (JUNV) were tested in A549 and Vero cell lines. It was found that treating infected cells with MPA-C decreased the JUNV yield and was more effective than free MPA in both cell line models for prolonged time treatments. Our results represent the first report of the antiviral activity of this type of BSA-MPA complex against JUNV, as assessed in cell culture model systems. MPA-C shows promise as a candidate for drug formulation against human pathogenic arenaviruses.

Increasing the polarity of β-lapachone does not affect its binding capacity with bovine plasma protein

Despite ortho-quinones showing several biological and pharmacological activities, there is still a lack of biophysical characterization of their interaction with albumin - the main carrier of different endogenous and exogenous compounds in the bloodstream. Thus, the interactive profile between bovine serum albumin (BSA) with β-lapachone (1) and its corresponding synthetic 3-sulfonic acid (2, under physiological pH in the sulphonate form) was performed. There is one main binding site of albumin for both β-lapachones (n ≈ 1) and a static fluorescence quenching mechanism was proposed. The Stern-Volmer constant (KSV) values are 104 M−1, indicating a moderate binding affinity. The enthalpy (−3.41 ± 0.45 and − 8.47 ± 0.37 kJ mol−1, for BSA:1 and BSA:2, respectively) and the corresponding entropy (0.0707 ± 0.0015 and 0.0542 ± 0.0012 kJ mol−1 K−1) values indicate an enthalpically and entropically binding driven. Hydrophobic interactions and hydrogen bonding are the main binding forces. The differences in the polarity of 1 and 2 did not change significantly the affinity to albumin. In addition, the 1,2-naphthoquinones showed a similar binding trend compared with 1,4-naphthoquinones.

Synthesis of dimeric indoles from Friedel–Crafts reaction of indoles with ketones catalysed by a Brønsted acid ionic liquid and their interactions with BSA and DNA

The synthesis of 35 dimeric indole derivatives was carried out by using [BCMIM][Cl] ionic liquid as a catalyst. The binding interaction between bovine serum albumin (BSA)/deoxyribonucleic acid (DNA) and synthesized compounds has been investigated.

Epicatechin attenuates lead (Pb)-induced cognitive impairment in mice: regulation on Nrf2 signaling pathway, and interference on the interaction between Pb with albumin

Epicatechin (EC) was used in this study to antagonize the cognitive dysfunction caused by lead (Pb) exposure in mice. Eight-week-old male Kunming mice were treated with PbCl2 (20 mg/kg) and/or EC (50 mg/kg) by gavage administration for 4 weeks. Morris water maze test showed that EC could improve memory dysfunction induced by Pb. EC antagonized Ca2+ overload, activated Nrf2 signaling pathway and reduced the accumulation of Pb in the brain and serum, which suggested that EC might alter Pb distribution in mice. In vitro, spectroscopic analysis, potentiometric titration and docking studies were applied to inquiry into the interaction between bovine serum albumin (BSA) and Pb2+ in presence or absence of EC. EC was proved to chelate Pb2+ and reduced the interaction between BSA and Pb2+. In summary, EC might protect Pb-induced cognitive impairment by activating Nrf2 signaling pathway, and suppressing Pb accumulation via interference on the binding of Pb to albumin.

3D Ag(I) coordination polymer sandwiched by water-muconate anionic layers: Synthesis, structure, Hirshfeld surface analysis, binding with BSA, and photocatalytic activity

The sonochemical reaction between silver salt, 1,3-bis(4-pyridylpropane (bpp) and trans,trans-muconic acid (H2muc) formed an Ag(I) coordination polymer with a 3D supramolecular sandwich architecture, {[Ag8(bpp)8(H2O)3].(muc)4.29(H2O)}n, (1) consisting of the silver-bpp cationic host that alternates with 2D water–muc guest anionic layers. The latter is formed by H-bonded water molecules-anions comprising hexagonal (H2O)6 clusters. The Hirshfeld surface and fingerprint plots have been used to quantify the weak intermolecular interactions in the crystal packing arrangement. The study showed that intermolecular hydrogen bonds are the most critical in constructing the titled supramolecular complex, accounting for 51.2% of the total Hirshfeld surface. Several spectrofluorimetric methods have been employed to investigate the binding interaction between Bovine Serum Albumin (BSA) and the titled complex. The complex induced significant fluorescence quenching of BSA, indicating a strong binding affinity for the protein. Static or ground state complex formation was envisaged as the primary quenching mechanism when the complex interacts with BSA. In addition, the Ag compound also offers photocatalytic properties by degrading the toxic organic methylene blue dye.

Association of bovine serum albumin and cetyltrimethylammonium chloride: An investigation of the effects of temperature and hydrotropes

Interactions between bovine serum albumin (BSA) and cetyltrimethylammonium chloride (CTAC) were studied utilizing conductivity approach. The critical micelle concentration (CMC), micelle ionization (α) along with counter ion binding (β) of CTAC micellization in aqueous solutions of BSA/BSA + hydrotropes (HYTs) have been computed at 298.15−323.15 K. Increase in temperatures of CTAC + BSA/BSA mixtures in HYTs resulted in elevation of CMC due to the association of chemical species in the respective systems which reduced the degree of micelle formation. CTAC + BSA consumed greater extents of surfactant species to generate micelle formation in the corresponding systems at higher temperatures. Standard free energy change ∆Gm0 associated with the assembling processes of CTAC in BSA was found negative suggesting the spontaneous nature of micellization processes. Magnitudes of ∆Hm0 and ∆Sm0 obtained from CTAC + BSA aggregation revealed the existence of H-bonding, electrostatic interactions along with hydrophobic forces among the constituents employed in the respective systems. ∆Gm0 The estimated thermodynamic parameters of transfer (free energy (∆Gm,tr0), enthalpy (∆Hm,tr0) and entropy (∆Sm,tr0)) and compensation variables (∆Hm0,∗ and Tc) provided significant insights on the association behaviors of the CTAC + BSA system in the selected HYTs solutions.

Elucidating the binding mechanism between bovine serum albumin and TiO2 nanoparticles with diverse properties: Insights from spectroscopic methods and molecular docking simulation

The interaction mechanism between bovine serum albumin (BSA) and titanium dioxide (TiO2) nanoparticles with different shapes, surface charge and hydrophobic properties was studied using multiple spectral methods and molecular docking simulation. UV–vis spectra showed that when BSA interacted with the four TiO2 NPs, the TiO2 nanoparticles and BSA formed a stable ground state complex. Fluorescence spectra showed that the binding capacities of four different types of TiO2 nanoparticles with BSA are as follows: spherical TiO2 (s-TiO2) > rod-shaped TiO2 (r-TiO2) > positively charged TiO2 (c-TiO2) > hydrophobic TiO2 (h-TiO2). The results of synchronous fluorescence, circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopy revealed that s-TiO2, r-TiO2, and c-TiO2 have a weak effect on the conformation of BSA, whereas h-TiO2 has a greater effect. Molecular docking and MD simulations results show that the content of hydroxyl groups plays a key role in the binding capacity.

Comparison of interfacial interactions between bovine serum albumin with water- and oil-soluble surfactants: An interfacial rheological study

The interfacial interactions between bovine serum albumin (BSA) with a water-soluble surfactant polyoxyethylene sorbitan monooleate (Tween 80) and an oil-soluble surfactant sorbitan monooleate (Span 80), respectively, were studied using the interfacial dilatational rheological experiments. The BSA molecules were irreversibly adsorbed at interface and formed a network with high dilatational modulus. The increasing interfacial pressure induced the transformation of BSA molecules from a compact globular to an unfolded flexible conformation, which enhanced the relaxation process. Tween 80 formed hydrophilic complexes with BSA in the aqueous phase, significantly slowing down the dynamic adsorption. In addition, Tween 80 played a dominant role at the interface due to its higher interfacial activity, thus inhibiting the interfacial performance of BSA. As BSA and Span 80 diffused towards the interface from different phases, they adsorbed rapidly at the interface and formed a mixed adsorption layer, thus exhibiting synergistic effects in decreasing the interfacial tension. However, the alternate arrangement of BSA and Span 80 at the interface disrupted the inter-protein interactions, resulting in a significant decrease in the dilatational modulus of the interfacial film. The obtained results showed that Span 80 from the oil phase and Tween 80 from the aqueous phase interacted with the protein in different ways, and thus presented distinct dynamic adsorption processes and interfacial performance. The present work provided a theoretical foundation for their practical application in food, cosmetic, and pharmaceutical industries.

Bovine Serum Albumin Interaction with Polyanionic and Polycationic Brushes: The Case Theoretical Study.

We apply a coarse-grained self-consistent field Poisson-Boltzmann framework to study interaction between Bovine Serum Albumin (BSA) and a planar polyelectropyte brush. Both cases of negatively (polyanionic) and positively (polycationic) charged brushes are considered. Our theoretical model accounts for (1) re-ionization free energy of the amino acid residues upon protein insertion into the brush; (2) osmotic force repelling the protein globule from the brush; (3) hydrophobic interactions between non-polar areas on the globule surface and the brush-forming chains. We demonstrate that calculated position-dependent insertion free energy exhibits different patterns, corresponding to either thermodynamically favourable BSA absorption in the brush or thermodynamically or kinetically hindered absorption (expulsion) depending on the pH and ionic strength of the solution. The theory predicts that due to the re-ionization of BSA within the brush, a polyanionic brush can efficiently absorb BSA over a wider pH range on the "wrong side" of the isoelectric point (IEP) compared to a polycationic brush. The results of our theoretical analysis correlate with available experimental data and thus validate the developed model for prediction of the interaction patterns for various globular proteins with polyelectrolyte brushes.

Pyridine derivatives complexes of Co(II) and Ni(II) 3‐bromobenzoates: Crystal structure, in silico anti‐SARS‐CoV‐2 potential, serum albumin binding properties and cytotoxicity

Two mononuclear [Co(3‐BrBA)2(NA)2(H2O)2] (1) and [Ni(3‐BrBA)2(3‐CNPY)2(H2O)2] (2) (3‐BrBA = 3‐bromobenzoate, NA = pyridine‐3‐carboxylic acid, and 3‐CNPy = 3‐cyanopyridine) were synthesized and characterized by single crystal X‐ray diffraction, elemental analysis, and FT‐IR spectroscopy. In both complexes, the metal atom is coordinated by two oxygen atoms of two carboxylate anions, two nitrogen atoms of two pyridine rings, and two oxygen atoms of two water molecules in the distorted octahedral environment. Intermolecular interactions were examined with the help of the 3D Hirshfeld surfaces and 2D fingerprint plots. With the help of density functional theory (DFT) studies, besides verifying the experimentally obtained structural properties, the electronic energies, polarizability, dipole moments, ionization potentials, electron affinities, electronegativity, chemical hardness, global softness, electrophilic indexes, HOMO‐LUMO orbitals, and band gaps were also calculated. In vitro cytotoxic activity of the complexes on primary peripheral blood mononuclear cells were evaluated using the MTT assay. Fluorescence quenching techniques and molecular docking studies were used to investigate the interaction between bovine serum albumin (BSA) and the complexes. The molecular docking study has been used to explain the interaction of complexes with spike proteins of beta variant (B.1.351), gamma variant (P.1), delta variant (B.1.617.2), kappa variant (B.1.617.1), and omicron variant (B.1.1.529) of coronavirus. Additionally, the pharmacokinetic and toxicological properties of the complexes have been computed using the SwissADME and ProTox‐II online databases, respectively.

Study of the interactions between lactic acid-based deep eutectic solvents and bovine serum albumin

The interactions between bovine serum albumin (BSA) and four lactic acid-based deep eutectic solvents (LADESs) were studied by spectroscopic and electrochemical methods under simulated physiological conditions.

Molecular interactions between bovine serum albumin (BSA) and trihalophenol: Insights from spectroscopic, calorimetric and molecular modeling studies

The issue of disinfection byproducts (DBPs) in the water has received critical attention due to the health effects on humans. In the water environment, interactions between bovine serum albumins (BSA), the most abundant water-soluble protein, and DBPs unavoidably occur. In this study, comparative binding interactions of two aromatic DBPs − 2,4,6-trichlorophenol (TCP) and 2,4,6-tribromophenol (TBP) with BSA were investigated systematically utilizing fluorescence spectrometry, UV absorption spectrometry, isothermal titration calorimetry and molecular docking approach. The fluorescence quenching results indicated that TCP/TBP could quench the endogenous fluorescence of BSA through static quenching mechanisms, and TBP showed a more substantial quenching effect. The binding constants were determined for TCP-BSA (3.638 × 105 L/mol, 303 K) and TBP-BSA (6.394 × 105 L/mol, 303 K) complexes, with TBP showing higher binding affinity than TCP. The thermodynamic study and docking analysis suggested that hydrogen bonding and van der Waals forces were the primary interaction forces. Both of TCP and TBP were located in the subdomain IIIA of BSA, and TBP could form more stable complex than TCP. The results of the present study contributed valuable information on the environmental behaviors of halophenols in water environment from perspectives of binding with BSA.

Interaction, bioaccessibility and stability of bovine serum albumin-gamma-oryzanol complex: Spectroscopic and computational approaches

The study explored the interaction mechanism between bovine serum albumin (BSA) and gamma-oryzanol (GO) by spectroscopic and computational approaches and the potential to enhance bioaccessibility and chemical stability of GO in the complex with BSA. Fluorescence spectroscopy showed that GO was bound to BSA with static quenching at a single binding site, being consistent with molecular docking results. Thermodynamic analysis and molecular dynamics simulation showed that electrostatic forces dominated interactions between BSA and GO. Besides, BSA-GO complex was more stable at pH 7.4 than at pH 2.0, with low root-mean-square deviation (2.57 Å vs 12.37 Å) and low binding energy (–424.23 kJ/mol at 277 K vs –188.55 kJ/mol at 277 K), but complex stability significantly decreased with increasing temperature. The bioaccessibility and stability of GO in the complex were significantly higher than those in water. This study provided theoretical support for developing proteins as delivery system for GO.