Protein Human Serum Albumin Research Articles

Purslane (Portulaca oleracea L.) as a novel green-bioreactor for expression of human serum albumin (HSA) gene.

Transgenic plants showed high potential to become a valuable and safe source of bio-compounds that can be used as therapeutics without any require for pooled human blood products. Human serum albumin (HSA) is one of the best-selling pharmaceuticals in the world because it is utilized for treating several acute illnesses, including hypovolemia, burns, and hemorrhage. This work was aimed to investigate the production of recombinant HSA (rHSA) protein in a plant-based expression platform. For this, we used in-planta and tissue culture-based Agrobacterium-mediated transformation (TCBAT) procedures to insert HSA gene into purslane (Portulaca oleracea L.) genome. The purslane seeds and leaves were infected with A. tumefaciens strain LBA4404 containing the HSA gene on pBI121 plasmid, and then regenerated into transgenic plant on MS medium. The qRT-PCR, southern hybridization, western blotting, and ELISA analysis were accomplished to corroborate the insertion and expression of HSA gene in transgenic plantlets. The molecular asses indicated that HSA gene was successfully transferred and expressed in purslane plants using in-planta and TCBAT methods. The first attempt to express rHSA in purslane resulted in a low-level accumulation of the protein in the transgenic plant shoots. Therefore, we used a synthetic 5'UTR (synJ) to enhance HSA transcript stability and translation efficiency. The results suggested that the synJ caused pronounced enhancement of rHSA expression rate. The highest amount of rHSA protein was recorded in transgenic purslane generated by TCBAT method (33.92 ± 4.31µg/g FW).

Binding of the anticancer Ti(IV) complex phenolaTi to serum proteins: Thermodynamic and kinetic aspects

Titanium(IV) anticancer complexes are promising candidates for treatment of various cancers, and previous studies have pointed to possible interactions between Ti(IV) anticancer complexes and the serum proteins albumin and transferrin. Herein, we explored the binding of phenolaTi, a leading diaminobis(phenolato)bis(alkoxo) Ti(IV) anticancer complex, to serum proteins, and derived the binding constants and thermodynamic parameters. The results were compared with those obtained for a salan Ti(IV) bis(isopropoxo) complex and titanocene dichloride, studied under similar conditions. Human serum albumin (HSA) binds phenolaTi in a spontaneous, exothermic process, with a dissociation constant (Kd) of 47 ± 7 μM at room temperature. In the presence of transferrin, the Kd of phenolaTi increases by 2-fold, reflecting the competition between the two proteins over the complex, which was more dominant for the other, less hydrolytically stable complexes tested. Examining the kinetics of the binding, it reaches a maximum after ca. 6 h, and the bond partially dissociates after 24–36 h, presumably due to partial ligand hydrolysis in the absence of cells; nevertheless, the proteins HSA and transferrin have a negligible effect on cytotoxicity after 72 h of incubation, with a possible negative impact on cell entry at short incubation periods. Overall, HSA serves as a carrier for phenolaTi through both its known drug binding sites, presumably in its intact form, which is the species that actively penetrates the cells and inflects cytotoxicity.

Interaction properties of biosynthesized cadmium sulphide quantum dots with human serum albumin: further investigation of antibacterial activities and sensing applications.

The synthesis of small-sized quantum dots (QDs) (1-10 nm) via the green route has garnered great interest regarding their prospective use in many biological applications (diagnosis, drug delivery and in vivo sensing); this is difficult to achieve using chemical synthesis methods, which produce larger size QD particles and also require hazardous reagents. Here, we synthesized biogenic cadmium sulphide (CdS) QDs using green tea extract as the reducing agent to produce particles that were homogeneous and a smaller size of 2-4 nm. We also elucidated the (a) protein binding, (b) antibacterial use and (c) sensing applications of biogenic CdS QDs in this present work. The biosynthesized CdS QDs were found to have extensive antibacterial activity against both Gram-negative Escherichia coli and Gram-positive Enterococcus faecalis bacterial strains. The introduction of QDs in biological medium can lead to the formation of protein-QD complexes; therefore we investigated the binding interaction of CdS QDs with the carrier protein human serum albumin (HSA) in vitro. The synthesized CdS QDs quenched the intrinsic fluorescence of HSA through a static quenching mechanism and the binding constant (Kb ) was in the order of 104 M-1 . It was also observed that the presence of biogenic CdS QDs affected the HSA-ligand interactions in vitro. The synthesized CdS made highly effective sensors for tetracycline, rifampicin, and bilirubin with limit of detection (LOD) values of 99, 141 and 29 ng/ml, respectively.

Biophysical, Biochemical, and Molecular Docking Investigations of Anti-Glycating, Antioxidant, and Protein Structural Stability Potential of Garlic.

Garlic has been reported to inhibit protein glycation, a process that underlies several disease processes, including chronic complications of diabetes mellitus. Biophysical, biochemical, and molecular docking investigations were conducted to assess anti-glycating, antioxidant, and protein structural protection activities of garlic. Results from spectral (UV and fluorescence) and circular dichroism (CD) analysis helped ascertain protein conformation and secondary structure protection against glycation to a significant extent. Further, garlic showed heat-induced protein denaturation inhibition activity (52.17%). It also inhibited glycation, advanced glycation end products (AGEs) formation as well as lent human serum albumin (HSA) protein structural stability, as revealed by reduction in browning intensity (65.23%), decrease in protein aggregation index (67.77%), and overall reduction in cross amyloid structure formation (33.26%) compared with positive controls (100%). The significant antioxidant nature of garlic was revealed by FRAP assay (58.23%) and DPPH assay (66.18%). Using molecular docking analysis, some of the important garlic metabolites were investigated for their interactions with the HSA molecule. Molecular docking analysis showed quercetin, a phenolic compound present in garlic, appears to be the most promising inhibitor of glucose interaction with the HSA molecule. Our findings show that garlic can prevent oxidative stress and glycation-induced biomolecular damage and that it can potentially be used in the treatment of several health conditions, including diabetes and other inflammatory diseases.

Spectroscopic and in silico approach to probe the binding interactions of irbesartan and human serum albumin

ObjectiveThe free and active concentration of drugs and thereby their pharmacokinetic properties are controlled by their binding to human serum albumin (HSA) protein. Irbesartan (IRB), an antihypertensive drug was aimed to be investigated in terms of its binding interactions with different sites of HSA using in silico molecular docking technique along with the commonly employed spectroscopic techniques. MethodsUsing FT-IR spectroscopy, the spectral shifting and intensity variations before and after complexation with IRB were studied for amide A, amide-I as well as amide-II of HSA. The absorbance of HSA with and without increasing concentrations of IRB was studied at 280 nm and the binding constant was determined using UV-spectroscopy. Molecular docking study was performed, and the types of interactions were predicted. ResultsThe IR spectra of IRB-HSA complex showed reductions in the intensities of amide-I and II bands as well as marked reduction in the α-helix content of HSA. The absorbance of HSA protein increased with increasing concentrations of drug. A binding constant value of 5.64 × 104 M−1 was calculated indicating good interaction. Molecular docking studies showed that IRB interacts more effectively with site-I of HSA through greater number of hydrogen bonds and strong π–charge (electrostatic) interactions than with site-II. ConclusionsThe spectroscopic and molecular docking techniques proved to be effective tools to study the drug-protein interaction which provided accurate results as evident from these studies. Studying drug-albumin interaction is of utmost importance as it directly influences the overall pharmacokinetics of the drugs including its distribution, metabolism and therefore the duration of action.

Detection of human serum albumin by room temperature nematic liquid crystals based on polarising microscopy, molecular docking and Raman spectroscopy

ABSTRACT Liquid crystal-based biosensors serve an essential role to detect biomolecules and chemical events as an effective, and simple detection tool. A biosensor that works on the principle of orientational reordering of liquid crystal molecules in presence of protein is reported. We employ a liquid crystal 4´-pentyl-4-biphenylcarbonitrile to detect the protein human serum albumin using multiple techniques. The composite of liquid crystal and protein forms nematic droplets. The transitions in the radial to bipolar configuration of the droplets are investigated via polarising optical microscopy. The detection limit is determined to be 100 µM. The interaction between protein and liquid crystal is performed through molecular docking . The binding sites, active residues, and binding energies are also calculated from the analysis. The binding energy required to bind 5CB with HSA at this site is −8.10 Kcal/mol. Raman spectroscopy is performed to determine the vibrational changes in the active residues, conformations of the disulphide bonds of the protein, which developed during the interaction with the liquid crystal. Raman spectroscopic studies confirm the interactions between the active residues of HSA and 5CB. The Raman parameters are studied at different HSA concentrations. This report demonstrates the applications of liquid crystals as transducing element in biosensing field.

Protein-Cloaked Nanoparticles for Enhanced Cellular Association and Controlled Pathophysiology via Immunosurveillance Escape.

Weak interactions play an important role in soft corona (SC) formation and thus help in evaluating the biological fate of the nanoparticles (NPs). Preadsorption of specific proteins on the NP surface, leading to SC formation, has been found to help NPs in evading immunosurveillance. However, the role of different preadsorbed biomolecules in determining the NP pathophysiology and cellular association, upon their re-exposure to in vivo conditions, still remains elusive. Here, differently charged gold NPs were precoated with two different blood components, viz. red blood cells and human serum albumin protein, and these were then re-exposed to human serum. Cloaking NPs with protein improved the NP colloidal stability and other physico-chemical properties along with increased cellular association. Detailed proteomic analysis suggested that protein-camouflaged NPs showed a decrease in immune-responsive proteins compared to their bare counterparts. Further, it was also observed that the secondary protein signature on the NP surface was governed by primary protein coating; however, the event was more or less NP charge-independent. This study will pave the path for future strategies to make NPs invincible to the immunosurveillance system of the body.

Understanding the partitioning of polyamines in micelles and delivery to the carrier protein: Thermodynamic approach

Micelle-based drug delivery system is widely used to solubilize and carry a varied range of drugs to the target cells. It selectively delivers drugs to the site of action and hence increases drug bioavailability and reduces the side effects of the drug. In the current work, we have studied the partitioning of two polyamines spermidine and spermine in hexadecyltrimethylammonium bromide (HTAB) micelles followed by their delivery to the carrier protein human serum albumin (HSA) using a combination of spectroscopy and calorimetry. The thermodynamic parameters for the partitioning of the polyamines with the micelles provide information about the nature of interactions of the polyamines with HTAB micelles and monomers. The ITC and docking results suggest that the polyamines sequentially bind with HSA with the values of binding constants in the range of 105 to 102. The binding of these polyamines with HSA gets slightly altered when delivered through HTAB micelles. Fluorescence and CD measurements suggest that the binding of these polyamines does not affect HSA conformation significantly. The results will help in understanding the mechanism of drug partitioning in micellar structures which is essential for developing guidelines to design effective drug delivery systems.

Comparative binding studies of bacosine with human serum albumin and α-1-acid glycoprotein biophysical evaluation and computational approach

Bacosine (BAC) is a natural product isolated from a herb and used in the Ayurvedic system of medicine. It is reported to have a wide array of biological activities, which has generated interest in its therapeutic potential. To better understand how BAC may operate as a potential anti-cancer therapeutic, we examined its anti-cancer properties in the human breast cancer cell line, MCF-7. In order to get an idea of how it may behave in vivo, we also evaluated its interaction with human serum albumin (HSA) and α-1-acid glycoprotein (AGP) using fluorescence spectroscopy and in silico molecular modelling. Based on our in vitro studies, we found that BAC inhibited MCF-7 cell growth in a dose-dependent manner with an IC50 value of 9 µM. In addition, the intrinsic fluorescence of HSA and AGP was quenched by BAC, consistent with a static quenching mechanism. Fluorescence emission spectroscopy revealed a binding of 2.97 ± 0.01 × 104 M−1 for HSA-BAC which corresponded to a free energy change of − 6.07 kcal/mol at 25 °C. In addition, we found that BAC had a binding constant of 1.8 ± 0.02 × 103 M−1 to AGP which corresponded to a change in free energy − 4.42 kcal/mol at 25 °C. We also identified the site of BAC binding to the HSA protein using the site-specific marker, phenylbutazone, along with molecular docking studies. Circular dichroism spectra revealed partial changes in the secondary structure of HSA in the presence of BAC suggesting direct interactions. Molecular dynamics simulations demonstrated that the HSA-BAC complex reaches an equilibration state at around 4 ns, suggesting that the HSA-BAC complex is quite stable. Our results provide evidence that serum proteins can act as a carrier protein for BAC, potentially impacting its development as an anti-cancer agent.

In‐situ Investigations on Gold Nanoparticles Stabilization Mechanisms in Biological Environments Containing HSA

AbstractNanoparticles (NPs) developments advance innovative biomedical applications. However, complex interactions and the low colloidal stability of NPs in biological media restrict their widespread utilization. The influence of NPs properties on the colloidal stability for gold NPs with 5 and 40 nm in diameter with two surface modifications, methoxy‐polyethylene glycol‐sulfhydryl (PEG) and citrate, in NaCl and human serum albumin (HSA) protein solution, is investigated. This study is based on small‐angle X‐ray scattering (SAXS) methods allowing the in‐situ monitoring of interactions in physiological conditions. The PEG coating provides high colloidal stability for NPs of both sizes. For 5 nm NPs in NaCl solution, a stable 3D self‐assembled body‐centered cubic (BCC) arrangement is detected with an interparticle distance of 20.7 ± 0.1 nm. In protein solution, this distance increases to 21.9 ± 0.1 nm by protein penetration inside the ordered structure. For citrate‐capped NPs, a different mechanism is observed. The protein particles attach to the NPs surfaces, and an appropriate concentration of proteins results in a stable suspension. Cryogenic transmission electron microscopy (Cryo‐TEM), UV–visible spectroscopy, and dynamic light scattering (DLS) support the SAXS results. The findings will pave the way to design and synthesize NPs with controlled behaviors in biomedical applications.

Design, synthesis and mechanistic studies of a TICT based fluorogenic probe for lighting up protein HSA

Human serum albumin (HSA) in blood serves as an important biomarker for clinical diagnosis, and fluorescence sensing method has attracted extensive attention. In this work, a small organic molecule probe, YS8, involving twisted intramolecular charge transfer (TICT) characteristic, was designed and investigated to detect HSA. YS8 kept silent state in fluorescence under physiological conditions, but the encapsulation of YS8 in the hydrophobic subdomain IB region of HSA inhibited the TICT state and produced a clear light-up fluorescent signal. Especially, YS8 was demonstrated to be an efficient fluorogenic probe to discriminate HSA from other proteins including the bovine serum albumin (BSA). Moreover, YS8/HSA complex could be applied in fluorescence imaging in living cells and is also useful in the study of artificial fluorescent protein (AFP).

Exploring the Molecular Level Interaction of Human Serum Albumin with Calcium Oxalate Monohydrate Crystals.

Human serum albumin (HSA) is one of the most abundant proteins in the blood plasma, urine as well as in the organic matrix of renal calculi. Macromolecules present in the urine modulate kidney stone formation either by stimulating or inhibiting the crystallization process. In the present study, the effect of HSA protein on the growth of calcium oxalate monohydrate crystal (COM) was investigated. Crystal growth assay was used to measure oxalate depletion in the crystal seeded solution in the presence of HSA. HSA concentrations exhibiting effect on crystal growth were selected for FTIR and XRD analysis. In silico docking was performed on seven different binding sites of HSA. Albumin plays dual role in the growth of calcium oxalate crystallization. FTIR and XRD studies further revealed HSA exerted strain over crystal thus affecting its structure by interacting with amino acids of its pocket 1. Docking results indicate that out of 7 binding pocket in protein, calcium oxalate interacts with Arg-186 and Lys-190 amino acids of pocket 1. Our study confirms the role of HSA in calcium oxalate crystallization where acidic amino acids arginine and lysine bind to COM crystals, revealing molecular interaction of macromolecule and crystal in urolithiasis.

Assessment of polyethersulfone and polyacrylonitrile hemodialysis clinical membranes: In situ synchrotron-based imaging of human serum proteins adsorption, interaction analyses, molecular docking and clinical inflammatory biomarkers investigations

While hemodialysis augments the physiological functions of the kidney in end stage renal disease (ESRD) patients, inherent membrane properties initiate life-threating biological episodes upon contact with blood. Membrane materials have different morphological and chemical properties that may become complement, leukocyte and even coagulation activators leading to several cardiovascular diseases due to biocompatibility issues upon contact with blood. The present study offers an in-depth understanding into two commonly used clinical polyethersulfone (PES) and polyacrylonitrile (PAN) membranes in Canadian hospitals and the effects of blood-membrane interactions on their biocompatibility, in terms of the initiation of blood activation and pro-inflammatory cytokine, from both experimental and theoretical standpoints. PES and PAN were thoroughly investigated to explore their susceptibility toward interaction with three human serum proteins. The extent of protein adsorption, and subsequent interactions on the membrane surfaces were investigated after ultrafiltration with human serum albumin (ALB), fibrinogen (FB) and transferrin (TR) proteins. The buildup of protein microparticles across different stratified membrane layers was probed using Synchrotron-based X-ray microtomography conducted with a biomedical imaging and therapy (BMIT 05ID-2) beamline at the Canada's national synchrotron light source facility. Furthermore, evidence of protein adhesion has been exhaustively investigated by surface chemical analyses and high-resolution surface imaging. The difference tendencies toward protein membrane-surface adhesion for both materials contributed to biological activations when studying in vitro clinical tests with inflammatory biomarkers using Human Magnetic Luminex assays of Serpin/ Antithrombin-III, Properdin, C5a, 1L-1α, 1L-1β, TNF-α, IL6, and vWF. Experimental results have been complemented with Molecular Modeling Docking analyses in the assessment of interaction patterns of human serum proteins in a view to understanding the relationship between functional group chemistry and membrane-surface bonding. Our models reveal inherent binding between PAN nitrogen atoms and protein-bound amino acids while the PES model proposes a contribution with its sulfone chemical groups as a prerequisite to membrane-surface binding resulting in high levels of complement and inflammation factors. The differences in protein adhesion between both clinical membrane modules are attributed to varying degrees of surface hydrophilicity as a direct factor of protein/membrane biocompatibility. Both membranes interacted differently with ALB, FB and TR, however, PAN membrane exhibited less affinity for protein adsorption and membrane-surface fouling.

Deep eutectic solvents as modulator on the micellization behaviour of cationic surfactants and potential application in human serum albumin aggregation

Deep eutectic solvents (DESs) have been utilized in many important applications in interdisciplinary research areas including the investigation of self-assembly of surfactants. In present study, the micellization behaviour of two conventional cationic surfactants i.e., tetradecyltrimethylammonium bromide (TTAB) and cetyltrimethylammonium bromide (CTAB) are investigated in aqueous DESs solutions with the help of surface tension, conductivity, UV–vis spectroscopy, fluorescence and dynamic light scattering (DLS) techniques. The synthesis of the DESs is done by simply mixing of choline chloride (ChCl) and urea/ethylene glycol (EG) in 1 : 2 mol ratio at 353 K temperatureand it is characterized by using FTIR technique. Various interfacial parameters and thermodynamic properties are evaluated by using tensiometric and conductometric methods. A noteworthy decrease in the critical micelle concentration (CMC) and increase in the aggregation number (Nagg) are observed in presence of DESs. Thus signifying that the micellization process of the surfactants is much favored in the DESs solutions and these are further supported by DLS results. DLS results show an increase in the micellar size for all the micellar systems in aqueous DESs solutions. More importantly, the micellar systems of the cationic surfactants within DESs solutions were also utilized for the study of their interaction with human serum albumin (HSA) to see how this albumin protein is behaving within the cationic micellar solutions in presence of DESs. UV–vis spectroscopic evidences show attractive results. It is noteworthy that the albumin protein HSA shows stronger binding affinity towards the DES-surfactants systems. The present work may further enhance the potential application of these neoteric green solvent systems composed of water-surfactant-DESs in the field of colloids, protein biophysics, nanoscience, which in turn will be highly applicable in the fields of synthesis, catalysis, and pharmaceutics etc.

Computational Analysis of the Binding Mechanism of GenX and HSA.

One PFOS alternative, ammonium 2,3,3,3-tetrafluoro-2-(heptafluoropropoxy) propanoate, known as GenX, was created to replace one of the original PFAS. This small and tough molecule has been found in surface water, groundwater, drinking water, rainwater, and air emissions in some areas in the United States. Recently, GenX has been shown to have an impact on several disease-related proteins in humans, and just like PFOS, it binds to human protein human serum albumin (HSA). In this paper, we reported four binding sites of GenX on HSA protein via docking and molecular dynamics simulation.

Exploring the binding mechanism and adverse toxic effects of persistent organic pollutant (dicofol) to human serum albumin: A biophysical, biochemical and computational approach

The organochlorine pesticide dicofol (DCF), a persistent organic pollutant, is used as acaricide worldwide. Considering its large consumption in the agriculture sector and potential toxic effects such as endocrine disruption, carcinogenicity, and environmental persistence are detrimental to human health. To take an extensive evaluation of its potential toxicity, the current study was aimed to explore the binding mechanism and adverse effect of DCF on human serum albumin (HSA) by using an array of biophysical techniques (UV–visible, fluorescence, 3D fluorescence, and circular dichroism spectroscopy), isothermal titration calorimetric (ITC), computational methods and biochemical approaches. Fluorescence quenching and UV–Visible spectra of the HSA-DCF system confirmed static quenching mechanism and complex formation between HSA and DCF. The thermodynamics results from ITC revealed DCF-HSA interaction was exothermic and spontaneous and involved hydrophobic interactions and hydrogen bonding. The esterase activity of HSA displayed constant Vmax and elevated Km values confirming DCF-HSA competitive interaction. Circular dichroism spectra results revealed structural changes in HSA protein on interaction with DCF. Furthermore, molecular-specific site marker and molecular modelling results affirmed that the binding Site of DCF is Site I of HSA. A significant carbonyl content level in DCF-HSA system suggested protein structure damage. This work is likely to add a better understanding of DCF toxicity in human health and helpful in fortifying the check on food safety.

Investigation on bindings of a binaphthoquinone derivative with serum albumin proteins by fluorescence spectroscopy

Binding of a binaphthoquinone derivative namely, 5a,5b-dimethyldibenzo[b,h]biphenylene-5,6,11,12(5aH,5bH,11aH,11bH)-tetraone (L, C 22 H 16 O 4 ) with bovine serum albumin (BSA) and human serum albumin (HSA) have been examined by using fluorescence spectroscopy. The fluorescence emission of the L is quenched upon addition of L to a solution of BSA or that of HSA, but the BSA has shown a higher affinity towards L over the HSA protein. A molecular docking study is also performed to suggest the sites of BSA for weak interactions to bind the L. The docking analysis, has revealed the N-H···O hydrogen bonds of L with different amino acid residues. The L is located at about 7.7Å away from the Trp-213 which is the fluorescent unit of the BSA suggesting the role of environment of the tryptophan residue to be an important to have changed the emission intensities.

Controlling Polymer Morphologies by Intramolecular and Intermolecular Dynamic Covalent Iron(III)/Catechol Complexation-From Polypeptide Single Chain Nanoparticles to Hydrogels.

Responsive biomaterials, tunable from the molecular to the macroscopic scale, are attractive for various applications in nanotechnology. Herein, a long polypeptide chain derived from the abundant serum protein human serum albumin is cross-linked by dynamic-coordinative iron(III)/catechol bonds. By tuning the binding stoichiometry and the pH, reversible intramolecular folding into polypeptide nanoparticles with controllable sizes is achieved. Moreover, upon varying the stoichiometry, intermolecular cross-links become predominant yielding smart and tunable macroscopic protein hydrogels. By adjusting the intra- and intermolecular interactions, biocompatible and biodegradable materials are formed with varying morphologies and dimensions covering several lengths scales featuring rapid gelation without toxic reagents, fast and autonomous self-healing, tunable mechanical properties, and high adaptability to local environmental conditions. Such material characteristics can be particularly attractive for tissue engineering approaches to recreate soft tissues matrices with highly customizable features in a fast and simple fashion.

Thermotropic liquid crystals in the detection of albumins through a microscopic, spectroscopic and computational approach

Liquid crystals (LCs) are a promising system of molecules for biosensing as a transducing agent for detecting protein human serum albumin (HSA). Herein, we investigate the detection of HSA by a liquid crystal 4′-octyl-4-biphenylcarbonitrile (8CB) intending to develop an LC-based biosensor. The change in the alignment of liquid crystal molecules in the presence of protein results in the transfigurations of the director through interactions. The limit of 8CB to detect HSA is found to be at a reliable concentration in the development of biosensors. The transition in the director configurations from radial to bipolar during the crystalline to the isotropic phase of the liquid crystals are studied under polarizing optical microscopy. These transitions confirm the detection of HSA by 8CB. The docking analysis depicts the interactions by which 8CB liquid crystal molecules bind with protein HSA. The binding energy, binding active residues and their distances between the docked residues of HSA and molecules of ligand 8CB are calculated by molecular docking. Temperature-dependent Raman spectroscopy is used to analyse the spectral behaviour of the interactions. The residues validated by molecular docking studies correlate well with the findings of Raman spectra for the interaction between 8CB and HSA.

Neuroprotection Mediated by Human Blood Plasma in Mouse Hippocampal Slice Cultures and in Oxidatively Stressed Human Neurons.

Neuroprotection from oxidative stress is critical during neuronal development and maintenance but also plays a major role in the pathogenesis and potential treatment of various neurological disorders and neurodegenerative diseases. Emerging evidence in the murine system suggests neuroprotective effects of blood plasma on the aged or diseased brain. However, little is known about plasma-mediated effects on human neurons. In the present study, we demonstrate the neuroprotective effect mediated by human plasma and the most abundant plasma–protein human serum albumin against oxidative stress in glutamatergic neurons differentiated from human neural crest-derived inferior turbinate stem cells. We observed a strong neuroprotective effect of human plasma and human serum albumin against oxidative stress-induced neuronal death on the single cell level, similar to the one mediated by tumor necrosis factor alpha. Moreover, we detected neuroprotection of plasma and human serum albumin against kainic acid-induced excitatory stress in ex vivo cultured mouse hippocampal tissue slices. The present study provides deeper insights into plasma-mediated neuroprotection ultimately resulting in the development of novel therapies for a variety of neurological and, in particular, neurodegenerative diseases.