Structure Of BSA Research Articles

Desalination of dye and protein by Ba2+/Ca2+ co-crosslinked alginate filtration membrane loaded on polypropylene non-woven

Calcium alginate hydrogel filtration membranes show excellent fouling resistance, but the poor mechanical properties and instability limit the use of the membranes. In this paper, sodium alginate was co-crosslinked with Ba2+ and Ca2+ to prepare barium alginate/calcium alginate composite hydrogel membrane loaded on polypropylene non-woven (Ba/CaAlg-PP). The morphology, structure, and swelling rate of the composite filtration membrane were characterized. The fracture strength of the Ba/CaAlg membrane reached a maximum value of 2.47 MPa. The rejection rates of Ba/CaAlg-PP membrane for Methyl blue and NaCl were close to 100 % and <8.0 %, respectively. Meanwhile, the flux of the Ba/CaAlg-PP membrane in dye/NaCl mixture was 43.2 L·m−2·h−1 and the selectivity coefficient of dye/NaCl reached 154.6. Ba/CaAlg-PP membranes exhibited excellent permeability, rejection and long-term stability in protein desalination. The results of simultaneous fluorescence spectroscopy and molecular dynamics simulations showed that the Ba2+ in the Ba/CaAlg-PP membrane did not disrupt the helical structure of BSA. The Ba/CaAlg-PP membrane has a wide range of applications prospect in proteins and dyes desalination.

Structural insights into the binding interaction between noraucuparin and bovine serum albumin: Implications for antibiotic design and function

Noraucuparin, a biphenyl phytoalexin, emerges as a promising drug candidate. Serum albumin plays a very important role in the in vivo transportation of drugs. The investigation delves into the binding interaction between noraucuparin and BSA employing comprehensive spectroscopic methods and molecular docking technique. UV–vis and FL spectrum results indicated that noraucuparin bond with BSA, and there was a new complex produced at the binding site II in domains IIIA (Ser-453 residue). The dissociation constants Kd from The ITC analysis was found to be 4.63 × 10−5 M at 298 K and 6.67 × 10−5 M at 310 K, showing 310 K is favorable for the combination of noraucuparin and BSA. The negative enthalpy (ΔH) and entropy (ΔS) values for the interaction revealed that the binding behavior was driven by hydrogen bonds. The results obtained from 3D fluorescence and CD spectrum illustrated that noraucuparin could change the secondary structure of BSA. According to molecule docking result, the binding energy of interaction is −7.09 kcal·mol−1. These revelations furnish a nuanced molecular-level comprehension of noraucuparin's mechanism of action on serum albumin. The discernments garnered from this study bear substantial reference significance and practical implications for ongoing lead compound exploration in antibiotics, particularly in vivo contexts.

Interaction of different chloro-substituted phenylurea herbicides (diuron and chlortoluron) with bovine serum albumin: Insights from multispectral study

In this work, the interaction between different chloro-substituted phenylurea herbicides (diuron (DIU) and chlortoluron (CHL)) and BSA were investigated and compared at three different temperatures (283 K, 298 K and 310 K) adopting UV–vis, fluorescence, and circular dichroism spectra. The quenching mechanism of the interaction was also proposed. The energy transfer between BSA and DIU/CHL was investigated. The binding sites of DIU/CHL and BSA and the variations in the microenvironment of amino acid residues were studied. The changes of the secondary structure of BSA were analyzed. The results indicate that both DIU and CHL can significantly interact with BSA, and the degree of the interaction between DIU/CHL and BSA increases with the increase of the DIU/CHL concentration. The fluorescence quenching of BSA by DIU/CHL results from the combination of static and dynamic quenching. The DIU/CHL has a weak to moderate binding affinity for BSA, and the binding stoichiometry is 1:1. Their binding processes are spontaneous, and hydrophobic interaction, hydrogen bonds and van der Waals forces are the main interaction forces. DIU/CHL has higher affinity for subdomain IIA (Site I) of BSA than subdomain IIIA (Site II), and also interacts with tryptophan more than tyrosine residues. The energy transfer can occur from BSA to DIU/CHL. By comparison, the strength of the interaction of DIU-BSA is always greater than that of CHL-BSA, and DIU can destroy the secondary structure of BSA molecules greater than CHL and thus the potential toxicity of DIU is higher due to DIU with more chlorine substituents than CHL. It is expected that this study on the interaction can offer in-depth insights into the toxicity of phenylurea herbicides, as well as their impact on human and animal health at the molecular level.

Simultaneous Purification of Human Interferon Alpha-2b and Serum Albumin Using Bioprivileged Fluorinated Ionic Liquid-Based Aqueous Biphasic Systems.

Interferon alpha-2b (IFN-α2b) is an essential cytokine widely used in the treatment of chronic hepatitis C and hairy cell leukemia, and serum albumin is the most abundant plasma protein with numerous physiological functions. Effective single-step aqueous biphasic system (ABS) extraction for the simultaneous purification of IFN-α2b and BSA (serum albumin protein) was developed in this work. Effects of the ionic liquid (IL)-based ABS functionalization, fluorinated ILs (FILs; [C​2C​1Im][C​4F​9SO​3] and [N​1112(OH)][C​4F​9SO​3]) vs. mere fluoro-containing IL ([C​4C​1Im][CF​3SO​3]), in combination with sucrose or [N​1112(OH)][H​2PO​4] (well-known globular protein stabilizers), or high-charge-density salt K​3PO​4 were investigated. The effects of phase pH, phase water content (%wt), phase composition (%wt), and phase volume ratio were investigated. The phase pH was found to have a significant effect on IFN-α2b and BSA partition. Experimental results show that simultaneous single-step purification was achieved with a high yield (extraction efficiency up to 100%) for both proteins and a purification factor of IFN-α2b high in the enriched IFN-α2b phase (up to 23.22) and low in the BSA-enriched phase (down to 0.00). SDS-PAGE analysis confirmed the purity of both recovered proteins. The stability and structure of IFN-α2b and BSA were preserved or even improved (FIL-rich phase) during the purification step, as evaluated by CD spectroscopy and DSC. Binding studies of IFN-α2b and BSA with the ABS phase-forming components were assessed by MST, showing the strong interaction between FILs aggregates and both proteins. In view of their biocompatibility, customizable properties, and selectivity, FIL-based ABSs are suggested as an improved purification step that could facilitate the development of biologics.

A novel approach to chiral separation: thermo-sensitive hydrogel membranes.

The application of membrane technology for separating chiral compounds is hindered due to the restricted availability of chiral recognition sites on the membrane surface. In this study, we propose a novel approach for chiral separation through a selector (bovine serum albumin, BSA) mediated thermo-sensitive membrane system. A thermo-sensitive hydrogel-coated membrane (termed PDTAN) was developed by anchoring poly(N-isopropylacrylamide) (PNIPAm) onto a polyethersulfone (PES) membrane through an adhesive and hydrophilic dopamine hydrochloride (PDA)/tannic acid (TA)/chitosan (Chi) intermediate layer. The results demonstrate outstanding chiral separation efficiency, achieving αL/D = 3.30 for D-phenylalanine (D-Phe) rejection at 40 °C on a BSA-mediated PDTAN membrane system, with significant stability and minimal fouling, surpassing previous findings. Moreover, the PDTAN membrane altered the selective properties of recognition sites in BSA, transitioning from rejecting L-Phe to rejecting D-Phe. Analysis using fourth-order derivative UV-vis, circular dichroism (CD), and in situ Fourier transform infrared spectroscopy (FTIR) techniques revealed a transition in the secondary structure of BSA from α-helix to β-sheet as the temperature increased. This transition, facilitated by hydrogen bonding between BSA and PNIPAm, enabled selective recognition of D-Phe, demonstrating a distinct shift in chiral recognition properties. Importantly, with D-Phe adsorbed onto β-sheet structures of BSA, hydrogen-bond interactions between BSA and the PDTAN membrane were significantly reduced, thereby minimizing membrane fouling and achieving the durability of membrane-based chiral separation.

Bovine Serum Albumin as a Platform for Designing Biologically Active Nanocarriers-Experimental and Computational Studies.

Due to the specificity of their structure, protein systems are adapted to carry various ligands. The structure of many proteins potentially allows for two types of immobilization of a therapeutic agent, either on the outer surface of the protein or within the protein structure. The existence of two active sites in BSA's structure, the so-called Sudlow I and II, was confirmed. The conducted research involved determining the effectiveness of BSA as a potential carrier of 5-fluorouracil (5FU). 5-fluorouracil is a broad-spectrum anticancer drug targeting solid tumors. The research was carried out to estimate the physicochemical properties of the system using complementary measurement techniques. The optimization of the complex formation conditions made it possible to obtain significant correlations between the form of the drug and the effective localization of the active substance in the structure of the protein molecule. The presence of two amino groups in the 5FU structure contributes to the deprotonation of the molecule at high pH values (pH > 8) and the transition to the anionic form (AN1 and AN3). To investigate the binding affinity of the tautomeric form with BSA, UV-vis absorption, fluorescence quenching, zeta potential, QCM-D, and CD spectroscopic studies were performed. The experimental research was supported by molecular dynamics (MD) simulations and molecular docking. The simulations confirm the potential location of 5FU tautomers inside the BSA structure and on its surface.

A deep-red fluorescent probe based on naphthalimide for discrimination of HSA from BSA and tracking HSA by bioimaging

The tertiary structures of HSA and BSA show a 76 % similarity, and the abnormal levels of HSA in body fluids can cause many diseases. Therefore, accurate quantification of HSA and effectively distinguishing HSA from BSA have significant application value in various fields. In this paper, a deep-red fluorescent probe, NITH, based on 1,8-naphthalimide, is demonstrated as a potential tool for accurately quantifying HSA and distinguishing HSA from BSA. The probe not only exhibits large stokes shift (100 nm) and low detection limit (4.61 μg/L, 0.0692 nM), but also effectively detects HSA by entering its hydrophobic cavity and emitting red fluorescence. Furthermore, NITH is capable of tracking the distribution levels of HSA within the cells through endogenous and exogenous cellular imaging. The application of NITH spans various environments such as cells, zebrafish, urine, and test strips, solidifying it as an effective tool for HSA detection.

New ionic liquids based on 5-fluorouracil: Tuning of BSA binding and cytotoxicity

In this work, we describe the synthesis, interactions with bovine serum albumin, and cytotoxicity of new ionic liquids based on 5-fluorouracil (API-ILs) with different cations (imidazolium, choline, isoquinolinium, guanidinium). The secondary and tertiary structure of BSA in solutions with different concentrations of API-ILs was monitored by the circular dichroism (CD) technique. The addition of API-ILs does not lead to structural changes in BSA. A quenching of fluorescence spectra intensity of BSA in presence of all API-ILs was observed, allowing the quantification of binding between API-ILs and BSA. The preferred localization of both ions in API-ILs differs significantly depending on the structure of the cation according to molecular docking. The aggregation of BSA in presence of API-ILs was analyzed by the dynamic light scattering (DLS) method, revealing a moderate increase in particle size. Cytotoxicity and selectivity of API-ILs on cancer and normal cell lines were estimated, showing a clear modification of the pharmaceutic activity of ionic liquid compared to 5-fluorouracil.

Complexation study of syringaldehyde complexed with serum albumin

As a major flavonoid polyphenolic compound in the stem of Hibiscus taiwanensis, syringaldehyde (SA) has numerous pharmacological effects. Nevertheless, owing to its less in-depth study, its application is limited. Within this work, the interactions between serum albumin and SA were elucidated by multispectral studies. The results of ultraviolet/visible absorption spectroscopy suggest that the conformation of serum albumin can be altered by binding with SA. Fluorescence spectroscopy indicates that SA forms complexes with serum albumin, quenching its fluorescence. This suggests that the fluorescent residues of serum albumin are situated at or near the binding site. Additionally, FT-IR results confirm that SA alters the secondary structure of BSA, specifically affecting the positions of both amide I and amide II bands. Via the computational biology analyses, it was confirmed that SA binds at the active site of serum albumin and nine residues form hydrophobic interactions. In addition, the cytotoxicity of SA to BRL-3A cells was also studied, and SA had almost no toxicity to the growth of BRL-3A cells. The complex has a higher α-amylase inhibition capacity than SA alone. To sum up, this work reveals that the interaction of SA with BSA induces a conformational alteration in BSA. It also proved that SA inhibits α-amylase more significantly and has great potential in hypoglycemia.

Bilingual Teacher Talk Pada Pengajaran TEYL di Sepama Kamboja

This study focuses on translation analysis of the use of bilingual teacher talk in teaching TEYL (Teaching English for Young Learners) in Sepama Cambodian classrooms. The method used is qualitative descriptive. The results showed that the students as teachers in the Sepama class used 8 translation techniques based on theories from Molina and Albirr. The results of the analysis were obtained based on the processing of 35 data obtained from online learning videos. The literal translation technique was applied to 9 data or 25.71%. Amplification technique as much as 2 data or 5.71%. Variation technique 1 data (2.85%), Typical matching technique 2 data or 5.71%. While the reduction technique has 9 data (25.71%). Transposition and particulate techniques each have 3 data or 8.57%. and finally Modulation technique as much as 4 data or 11.43%. The reduction technique is widely used because the structure of BSa is simpler than BSu. While literal techniques are also often used because teachers must immediately convey BSa and BSu immediately respectively.

MRI Directed Magnevist Effective to Study Toxicity of Gd-Doped Mesoporous Carbon Nanoparticles in Mice Model.

Magnetic resonance imaging (MRI) has been a valuable and widely used examination technique in clinical diagnosis and prognostic efficacy evaluation. The introduction of MRI contrast agent (CA) improves its sensitivity obviously, particularly with the development of nano-CA, which presents higher contrast enhancement ability. However, systematical evaluation of their toxicity is still limited, hampering their further translation in clinics. In this paper, to systematically evaluate the toxicity of nano-CA, Gd-doped mesoporous carbon nanoparticles (Gd-MCNs) prepared by a one-step hard template method were introduced as a model and clinically used MRI CA, Magnevist (Gd-DTPA) as control. Their in vitro blood compatibility, cellular toxicity, DNA damage, oxidative stress, inflammation response as well as in vivo toxicity and MR imaging behaviors were studied and compared. The experimental results showed that compared with Gd-DTPA, Gd-MCNs displayed negligible influence on the red blood cell shape, aggregation, BSA structure, macrophage morphology and mitochondrial function. Meanwhile, limited ROS and inflammatory cytokine production also illustrated the cellular compatibility of Gd-MCNs. For in vivo toxicity evaluation, Gd-MCNs presented acceptable in vivo biosafety even under 12 times injection for 12 weeks. More importantly, at the same concentration of Gd, Gd-MCNs displayed better contrast enhancement of tumor than Gd-DTPA, mainly coming from its high MRI relaxation rate which is nearly 9 times that of Gd-DTPA. In this paper, we focus on the toxicity evaluation of MRI nano-CA, Gd-MCNs from different angles. With Gd-DTPA as control, Gd-MCNs appeared to be highly biocompatible and safe nanoparticles that possessed promising potentials for the use of MRI nano-CA. In the future, more research on the long-term genotoxicity and the fate of nanoparticles after being swallowed should be performed.

Hydroxychloroquine-Loaded Chitosan Nanoparticles Induce Anticancer Activity in A549 Lung Cancer Cells: Design, BSA Binding, Molecular Docking, Mechanistic, and Biological Evaluation.

The current study describes the encapsulation of hydroxychloroquine, widely used in traditional medicine due to its diverse pharmacological and medicinal uses, in chitosan nanoparticles (CNPs). This work aims to combine the HCQ drug with CS NPs to generate a novel nanocomposite with improved characteristics and bioavailability. HCQ@CS NPs are roughly shaped like roadways and have a smooth surface with an average size of 159.3 ± 7.1 nm, a PDI of 0.224 ± 0.101, and a zeta potential of +46.6 ± 0.8 mV. To aid in the development of pharmaceutical systems for use in cancer therapy, the binding mechanism and affinity of the interaction between HCQ and HCQ@CS NPs and BSA were examined using stopped-flow and other spectroscopic approaches, supplemented by molecular docking analysis. HCQ and HCQ@CS NPs binding with BSA is driven by a ground-state complex formation that may be accompanied by a non-radiative energy transfer process, and binding constants indicate that HCQ@CS NPs-BSA was more stable than HCQ-BSA. The stopped-flow analysis demonstrated that, in addition to increasing BSA affinity, the nanoformulation HCQ@CS NPS changes the binding process and may open new routes for interaction. Docking experiments verified the development of the HCQ-BSA complex, with HCQ binding to site I on the BSA structure, primarily with the amino acids, Thr 578, Gln 579, Gln 525, Tyr 400, and Asn 404. Furthermore, the nanoformulation HCQ@CS NPS not only increased cytotoxicity against the A549 lung cancer cell line (IC50 = 28.57 ± 1.72 μg/mL) compared to HCQ (102.21 ± 0.67 μg/mL), but also exhibited higher antibacterial activity against both Gram-positive and Gram-negative bacteria when compared to HCQ and chloramphenicol, which is in agreement with the binding constants. The nanoformulation developed in this study may offer a viable therapy option for A549 lung cancer.

Multi-spectroscopies and molecular simulation insights into the binding of bovine serum albumin and sodium tripolyphosphate

Sodium tripolyphosphate (STPP) is an odorless and water-soluble anionic mineral compound. STPP is used as a separator, texturizer, emulsifier and buffer in the food and detergent industries. Considering the importance of the topic and the interaction of food additives with biological molecules including blood serum albumin, we investigated the binding properties of STPP food additive to blood serum albumin through UV–Vis spectroscopy, fluorescence spectroscopy, Fourier transform infrared spectroscopy (FT-IR), and molecular docking analysis. According to the results, after forming a complex with BSA, STPP reduced the fluorescence intensity of BSA through static quenching mechanisms, and the UV–Vis absorption results were also confirmatory. Synchronous fluorescence and FT-IR results showed that the microenvironment and secondary structure of BSA changed in the presence of STPP. The synchronous fluorescence study has shown that the quenching toward Trp residue is higher than Tyr residue. The thermodynamic results showed that van der Waals force and hydrogen bonding play the main roles in the formation of the STPP-BSA complex. The binding constant decreases from 2.23 × 106 to 4.25 × 101 (M−1) with increasing temperature, indicating a decrease in complex formation due to the interaction of STPP with BSA. Furthermore, molecular docking studies showed that STPP binds to the cavity between domains IIIA and IIIB by van der Waals forces and hydrogen bonds through residues Ser 418, Thr 419, Tyr 496, Lys 499, and Lys 533.

Biological Evaluation and Binding Mechanism of 5-HT7 Specific Arylpiperazinyl-Alkyl Benzothiazolone: Radiobiology and Photo-physical Studies.

Diversely substituted methoxy derivatives of arylpiperazinyl-alkyl benzothiazolone has been evaluated as specific probe for 5HT7. To determine the best methoxy derivative for 5HT7 receptor affinity, we synthesised a number of 2-benzothiazolone arylalkyl piperazine derivatives. In-vitro/vivo studies with C-2 substituted [11C]ABT showed 5HT7 specific binding. The radiochemical purity of [11C]ABT was found to be more than 99% with radiochemical stability persistence for more than 1.5 hr at 25 °C. The interaction of BSA and ABT has been analysed by photophysical studies for better understanding of properties such as adsortion, distribution, metabolism and elemination (ADME). The interaction between ABT and BSA was analyzed by using the UV-vis and fluorescence spectra. UV-vis spectra analyzed the changes in primary structure of BSA on its interaction with ABT. ABT showed quenched fluorescence emission intensity of tryptophan residues in BSA via static quenching mechanism. This study might help to understand how ABT binds to serum protein or subsequently to know the ADME of this drug candidate.

Kinetic and thermodynamic aspects on the interaction of serum albumin with sodium hydrosulfite: Spectroscopic and molecular docking methods

Sodium hydrosulfite is a sulfur-containing food additive that is used as a decolorizing agent in the sugar industry to purify syrup and remove natural color compounds obtained from sugar beet, sugar cane, and color compounds created during production. Recent studies show gastrointestinal, aspiration, skin and eye complications from excessive use of sulfur-containing compounds. According to recent studies and the importance of investigating the interaction of food additives with biological molecules, we also investigated the binding properties of sodium hydrosulfite to blood serum albumin through UV–Vis spectroscopy, fluorescence spectroscopy, competitive binding experiments, Fourier transform infrared spectrometry (FT-IR), surface plasmon resonance (SPR), and molecular simulation analysis. According to the results, Sodium hydrosulfite decreased the fluorescence intensity of BSA through both static and dynamic quenching mechanisms after forming a complex with BSA. The results of synchronous fluorescence and FT-IR demonstrated that the microenvironment and the secondary structure of BSA were changed in the presence of sodium hydrosulfite. The negative values of ΔH° and ΔS° indicated that van der Waals force or hydrogen bonding is the main factor of binding between sodium hydrosulfite and BSA. The result of UV–Vis spectroscopy confirmed the binding of sodium hydrosulfite to BSA. Binding constant decreases from 13.06 to 0.24 (103 M−1) with increasing temperature, which indicates a decrease in complex formation owing to the interaction of sodium hydrosulfite with BSA. Molecular docking experiments confirm the binding tendency of sodium hydrosulfite to a cavity between domains II and III (Site I and Site II) through residues Cys460, Cys476, Asn457, Arg483, Lys204, and Ala200 with a binding energy of −12.86 kJ mol−1.

Enantioselective effect of chiral prothioconazole on the conformation of bovine serum albumin

As a typical chiral triazole fungicide, the enantioselective toxicity of prothioconazole to environmental organisms is of increasing concern. Herein, the binding mechanism of chiral PTCs to BSA was investigated by multi-spectral technique and molecular docking. Fluorescence titration and fluorescence lifetime experiments fully established that quenching BSA fluorescence by chiral PTCs is static quenching and could spontaneously bind to BSA. Hydrophobic interactions dominate the binding process of chiral PTCs to BSA. Differently, although both chiral PTCs and BSA have a primary binding site, the difference in chiral isomerism leads to a stronger binding ability of S-PTC than R-PTC. Both configurations of PTC can change the conformation of BSA and induce changes in the microenvironment around its amino acid residues, and the effect of S-PTC is more significant. Overall, S-PTC exhibited a more substantial effect on BSA structure relative to R-PTC. That is, S-PTC may lead to more potent potential toxicological effects on environmental organisms. This study provides a comprehensive assessment of the environmental behavior of chiral pesticides and their potential toxicity to environmental organisms at the molecular level and provides a theoretical basis for the screening of highly effective and biologically less toxic enantiomers of chiral pesticides.

Proteinosomes via Self-Assembly of Thermoresponsive Miktoarm Polymer Protein Bioconjugates.

To fabricate nanoscale proteinosomes, thermoresponsive miktoarm polymer protein bioconjugates were prepared through highly efficient molecular recognition between the β-cyclodextrin modified BSA (CD-BSA) and the adamantyl group anchored at the junction point of the thermoresponsive block copolymer poly(ethylene glycol)-b-poly(di(ethylene glycol) methyl ether methacrylate) (PEG-b-PDEGMA). PEG-b-PDEGMA was synthesized by the Passerini reaction of benzaldehyde-modified PEG, 2-bromo-2-methylpropionic acid, and 1-isocyanoadamantane, followed by the atom transfer radical polymerization of DEGMA. Two block copolymers with different chain lengths of PDEGMA were prepared, and both self-assembled into polymersomes at a temperature above their lower critical solution temperatures (LCST). The two copolymers can undergo molecular recognition with the CD-BSA and form miktoarm star-like bioconjugates. The bioconjugates self-assembled into ∼160 nm proteinosomes at a temperature above their LCSTs, and the miktoarm star-like structure has a great effect on the formation of the proteinosomes. Most of the secondary structure and esterase activity of BSA in the proteinosomes were maintained. The proteinosomes exhibited low toxicity to the 4T1 cells and could deliver model drug doxorubicin into the 4T1 cells.

Investigation of the separate and simultaneous bindings of warfarin and fenofibrate to bovine serum albumin

Lipid-lowering drugs are often taken with anticoagulant drugs in hyperlipidemia patients. Fenofibrate (FNBT) and warfarin (WAR) are common clinical lipid-lowering drugs and anticoagulant drugs, respectively. A study of binding affinity, binding force, binding distance, and binding sites was performed to determine the interaction mechanism between drugs and carrier proteins (bovine serum albumin, BSA), as well as their effects on BSA conformation. Both FNBT and WAR can form complexes with BSA by van der Waals force and hydrogen bonds. WAR had a stronger fluorescence quenching effect on BSA, a stronger binding affinity, and greater effects on BSA conformation than FNBT. According to fluorescence spectroscopy and cyclic voltammetry, co-administration of drugs decreased one drug's binding constant to BSA and increased its binding distance. This suggested that each drug's binding to BSA was disturbed by each other, as well as each drug's binding ability to BSA was altered by the other. It was demonstrated that co-administration of drugs had greater effects on the secondary structure of BSA and microenvironment polarity surrounding amino acid residues, using multiple spectroscopy techniques, such as ultraviolet spectroscopy, Fourier transform infrared spectroscopy, and synchronous fluorescence spectroscopy.

Assessing the impact of choline chloride and benzyltrimethylammonium chloride-based deep eutectic solvents on the structure and conformational dynamics of bovine serum albumin: a combined steady-state, time-resolved fluorescence and fluorescence correlation spectroscopic study.

Although deep eutectic solvents (DESs) are regarded as useful substitutes for both ionic liquids and common organic solvents for storage and applications of biomolecules, it is still unclear whether all DESs or only specific types of DESs will be suitable for the said purpose. In view of this, the current study aims to report on the structure and conformational dynamics of BSA in the presence of two DESs, namely ethaline (choline chloride:ethylene glycol) and BMEG (benzyltrimethyl ammonium chloride:ethylene glycol), having the same hydrogen bond donor but with a distinct hydrogen bond acceptor, so that how small changes in one constituent of a DES alter the protein-DES interaction at the molecular level can be understood. The protein-DES interaction is investigated by exploiting both ensemble-averaged measurements like steady-state and time-resolved fluorescence spectroscopy, circular dichroism (CD) spectroscopy, and single-molecule sensitive techniques based on fluorescence correlation spectroscopy (FCS). Interestingly, the results obtained from these studies have demonstrated that while a very small quantity of BMEG completely unfolds the native structure of the protein, it remains in a partially unfolded state even at very high ethaline content. More interestingly, it has been found that at very high concentrations of BMEG, the unfolded protein undergoes enhanced protein-protein interaction resulting in the aggregation of BSA. All of the results obtained from these investigations have essentially suggested that both protein-DES interaction and interspecies interaction among the constituent of DESs play a crucial role in governing the overall stability and conformational dynamics of the protein in DESs.

Evaluation the binding of chlorogenic acid with bovine serum albumin: Spectroscopic methods, electrochemical and molecular docking

Chlorogenic acid(CGA) is the common active phenolic acid in Chinese medicinal materials such as honeysuckle and eucommia. It is a class of small molecules with multiple activities such as antioxidant, inhibiting cancer cells, lowering blood sugar and lowering blood pressure. In this paper, UV–vis spectroscopy, fluorescence spectroscopy, circular dichroism, molecular dynamics simulation and cyclic voltammetry (CV) electrochemical analysis were used to investigate the mechanism about interaction between CGA and BSA. Based on fluorescence quenching analysis, CGA quenched the inherent fluorescence of BSA remarkably through a static mechanism. The obtained value of binding constant (Kb = 5.75 × 105 L·mol−1) revealed a high binding affinity between CGA and BSA. The simulated molecular docking showed that hydrophobic force were also involved in the interaction between BSA and CGA. This paper also investigate the effect of temperature and metal ions on the binding of CGA and BSA. When the temperature increased, the binding of BSA and CGA was destroyed. Metal ions affect both the structure of BSA and the combination of BSA and CGA. By studying the mechanism of CGA interaction with BSA, we elucidated the storage and transport mechanism of CGA in vivo under simulated human environment and temperature conditions.