Serum Albumin Complex Research Articles

N-ethyl-2-pyrrolidinone substitution enhances binding affinity between tea flavoalkaloids and human serum albumin: Greatly influenced by esterization

Formation of catechins-human serum albumin (HSA) complex contributes to stably transporting catechins and regulating their bioavailability. Recently, a new class of catechins namely flavoalkaloids have been reported from tea. The unique structural modification with an N-ethyl-2-pyrrolidinone ring at catechins from these flavoalkaloids has raised our interest in their HSA binding affinity. Thus, we investigated the interaction between HSA and flavoalkaloids by molecular docking, UV-Vis spectroscopy (UV), fluorescence quenching approaches, and surface plasmon resonance (SPR). Thermodynamic parameters suggest that electrostatic forces contribute greatly to the interaction. The binding ability is affected by different ester group (galloyl or cinnamoyl) at 3-OH, N-ethyl-2-pyrrolidinone substituted position (C-6 or C-8), C-2, C-3 and C-5′'' configurations, and hydroxyl group numbers at B ring, among which the 3-O-cinnamoyl substitution and 5′''-R configuration present the strongest contributions. UV showed slight changes in the conformation and microenvironment of HSA during the binding process. The quenching and binding constants suggest that the quenching is a static type. The small KD values (1–20 μM) detected by SPR confirmed the strong binding affinities between HSA and flavoalkaloids. Present study will help us to understand the interaction mechanism between flavoalkaloids and HSA, shedding light on structural modification of common catechins to enhance the stability, bioavailability and bioactivities.

Sensitive, Color-Indicating and Labeling-Free Multi-Detection Cholesteric Liquid Crystal Biosensing Chips for Detecting Albumin.

A novel device for cholesteric liquid crystal (CLC)-based microfluidic chips, accommodated in a polydimethylsiloxane material, was invented. In this device, the reorientation of the CLCs was consistently influenced by the surface of the four channel walls and adjacent CLCs. When the inside of the microchannel was coated with the alignment layer, the CLCs oriented homeotropically in a focal conic state under cross-polarizers. Once antigens had bound onto antibodies immobilized onto the orientation sheet-coated channel walls, the light intensity of the CLC molecules converted from a focal conic state to a bright planar state caused by disrupting the CLCs. By means of utilizing pressure-propelling flow, the attachment of antigen/antibody to the CLCs should be detectable within consecutive sequences. The multi-microfluidic CLC-based chips were verified by measuring bovine serum albumin (BSA) and immune complexes of pairs of BSA antigen/antibody. We showed that the multiple microfluidic immunoassaying can be used for measuring BSA and pairs of antigen/antibody BSA with a detection limit of about 1 ng/mL. The linear range is 0.1 μg/mL–1 mg/mL. A limit of immune detection of pairs of BSA antigens/antibodies was 10 ng/mL of BSA plus 1000 ng/mL of the anti-BSA antibodies was observed. According to this innovative creation of immunoassaying, an unsophisticated multi-detection device with CLC-based labeling-free microfluidic chips is presented.

Toxic metal ion sequestration by amyloid-mediated fast coacervation

Summary Biomass materials have gained considerable attention as sustainable and renewable resources for the production of adsorbents. However, there remain significant challenges to their application scale-up, such as complex production or processing methods, poor stability, high cost, and low adsorption capacity. Herein, we report an environmentally friendly protein-polysaccharide complex that exhibits excellent removal efficiency of toxic metal ions. Through amyloid-mediated coacervation, the bovine serum albumin (BSA) and sodium carboxymethyl cellulose (CMC) complex, which can be formed within 1 min. The adsorbent is effective for the simultaneous removal of multiple toxic metal ions species (Hg2+, Cr3+, Pb2+, Cd2+, As3+, Ni2+, and Co2+) and radioactive elements (uranium) from tap water (at

Stability of spectrofluorimetric spectra of hematoporphyrin–serum albumin complexes: in vitro study

IntroductionHematoporphyrin is a photosensitizer used in photodynamic therapy of various malignant diseases. It is carried to the cancer tissue by serum albumins. Spectrofluorimetric spectra of hematoporphyrin–serum albumin complexes were examined in vitro.Material and methodsThe chemicals were: hematoporphyrin, human serum albumin and bovine serum albumin. The spectra were recorded on a Kontron SFM-25 Instrument AG at two excitation wavelengths: ex = 280 nm and ex = 295 nm. The spectra of hematoporphyrin 1.5 × 10–5 M as well as spectra of complexes of hematoporphyrin–human serum albumin (1.5 × 10–5 M Hp – 1.25 × 10–6 M HSA) and hematoporphyrin–bovine serum albumin (1.5 × 10–5 M Hp – 3.5 × 10–7 M BSA) were recorded repetitively for 8 days and compared to the initial spectrum.ResultsFormation of a complex with human serum albumin extends the stability of the hematoporphyrin spectrum. This extension is greater at excitation ex = 295 nm. Different stability of complexes with bovine and human serum albumins most likely does not result from an actual lower stability of bovine serum albumin complexes, but from the fact that dissimilarity in the structure of both albumins enables additional spectroscopic observations within subdomain IB in the bovine serum albumin molecule.ConclusionsSpectrofluorimetric spectra are stable longer when hematoporphyrin forms a complex with human serum albumin. The present data may be important for understanding the mechanism of hematoporphyrin transportation to the target cancer tissue and effectiveness of photodynamic therapy.

Interaction of Detonation Nanodiamonds with Hispidin

Hispidin is a secondary metabolite found in numerous medicinal mushrooms that has attracted significant attention, owing to its distinct biological effects, including antioxidant, anti-inflammatory, antitumor, and cytoprotective properties. Experiments are being carried out to study the interaction of detonation nanodiamonds (DNDs) with synthetic and natural hispidin sourced from extracts of Pholiota sp. fungus. The bioluminescence method is used to determine the adsorption/ desorption properties of DNDs toward hispidin. It is found that hispidin forms strong conjugates with DNDs, and the use of various eluents does not result in a significant release of the adsorbed hispidin molecules. DND-bovine serum albumin (BSA) complex, where DNDs serve as a carrier for the protein and the latter acts as a hispidin sorbent, has been developed and applied in hispidin adsorption/desorption tests. The results support the use of the DNDs as a carrier for hispidin in medical applications. They also advocate the application of the DND-BSA complex for isolating the substance from fungal extracts.

Molecular determinants of vascular transport of dexamethasone in COVID-19 therapy.

Dexamethasone, a widely used corticosteroid, has recently been reported as the first drug to increase the survival chances of patients with severe COVID-19. Therapeutic agents, including dexamethasone, are mostly transported through the body by binding to serum albumin. Here, the first structure of serum albumin in complex with dexamethasone is reported. Dexamethasone binds to drug site7, which is also the binding site for commonly used nonsteroidal anti-inflammatory drugs and testosterone, suggesting potentially problematic binding competition. This study bridges structural findings with an analysis of publicly available clinical data from Wuhan and suggests that an adjustment of the dexamethasone regimen should be further investigated as a strategy for patients affected by two major COVID-19 risk factors: low albumin levels and diabetes.

Dynamic Surface Properties of Solutions of Bovine Serum Albumin Complexes with Silica Nanoparticles

Surface properties of aqueous dispersions of bovine serum albumin complexes with silica nanoparticles have been studied using a set of methods that are sensitive to changes in the structure and composition of surface layers. In spite of the similar charges of the components, their interaction leads to changes in the surface properties of the dispersions; namely, the rates of variations in the dynamic surface elasticity and dynamic surface tension decrease due to the high electrostatic barrier of adsorption. The addition of an electrolyte decreases the electrostatic barrier. In this case, the adsorption of the complexes leads to a growth in the dynamic surface elasticity from the values characteristic of pure bovine serum albumin solutions (~80 mN/m) to 170 mN/m, which corresponds to the formation of macroscopically homogeneous adsorption film of nanoparticle–protein complexes.

Response of the subtropical forest soil N transformations to tannin acid-organic nitrogen complexes

It is well known that the hydrolysable tannin (tannin acid) and condensed tannins in a plant can influence the availability of soil nitrogen (N) through the formation of tannin–organic N complexes. However, the lack of research on the effect of tannin acid–organic N complexes on soil N hinders our understanding of the subsequent role of these complexes. In this line, an incubation experiment was carried out with the addition of tannin acid-arginine and tannin-bovine serum albumin (BSA) complexes, where tannin acid was represented as the hydrolysable tannin. For the necessary comparisons, tannin acid, arginine, or BSA was added to the soil samples. The results showed that tannic acid addition quickly decreased protein contents at the beginning of incubation and decreased soluble organic N (SON) after 3 days to produce the inorganic N in the soil as compared to control. Tannin-arginine complexes increased NH4+–N compared with control and this increased degree was found lower than arginine treatment. Moreover, the addition of tannin–BSA complexes did not significantly increase soil NH4+–N as BSA alone treatment did. NO3−–N and N2O emission increased in each treatment compared with control indicating nitrification was not limited. The increase of NH4+–N was mainly attributed to the decrease of SON after 3 days of incubation. These results suggested that tannin acid quickly formed the complexes with protein to impact soil N. While, the effects of tannin-arginine and tannin–BSA complexes on soil N transformation were quite dissimilar. Thus, this study highlighted the subsequent role of tannin–organic N complexes under the influence of tannin. Tannin and tannin–organic N complexes naturally coexist in the ecosystem to impact soil N dynamics and may interact with each other as well.

Indocyanine green-loaded injectable alginate hydrogel as a marker for precision cancer surgery.

Accurate identification of tumor sites and boundaries is of paramount importance during minimally invasive surgery. Although laparoscopic resection is being increasingly and widely performed for early gastric and colorectal cancers, the detection of tumors located inside the stomach and intestine is difficult owing to the lack of tactile sensation. Here, we propose the application of an indocyanine green (ICG)-loaded alginate hydrogel system as a fluorescence surgical marker for precise laparoscopic operations. A physical complex of ICG and human serum albumin (HSA) was mixed with sodium alginate to form an injectable hydrogel system. Calcium carbonate and D-gluconic acid (GA) were added to the gel to control its strength and gelation time, respectively. The optimal conditions for the preparation of injectable hydrogels were determined by analyzing the fluorescence spectra and sol-gel transition time of the prepared samples at various concentrations and compositions. Next, the aqueous solutions of ICG, ICG-HSA, and ICG-HSA-loaded alginate were subcutaneously injected into nude mice (three mice per group), and near-infrared (NIR) fluorescence images of the mice (λex. =780 nm, λem. =845 nm) were obtained at different points in time for 8 days. Then, fluorescence intensities at the injection sites, target-to-background ratio, and areas of ICG fluorescence were analyzed. Finally, the potential utility of ICG-HSA-loaded alginate hydrogel as a surgical marker was evaluated in a porcine model. The ICG-HSA-loaded alginate solution was injected into three sites in the submucosal space of the porcine stomach via a catheter. A fluorescent laparoscopic system was installed on the abdomen of the pig 3 days post-injection, and the fluorescence signal generated from the fluorescence surgical marker located inside the stomach was evaluated using the fluorescence laparoscope system (λex. =785 nm, λem. =805 nm). The optimal concentration of ICG-HSA complex was determined to be 30 µM, and maximum fluorescence intensity of the complex was obtained at a 1:1 mole ratio of HSA to ICG. The subcutaneous injection of ICG or ICG-HSA solution in mice resulted in the rapid spread of the fluorescence signal around the injection site in 3 h, and a weak fluorescence was detected at the injection site 24 h post-injection. In contrast, the fluorescence detection time was effectively prolonged up to 96 h post-injection in the case of ICG-HSA-loaded alginate gel, while diffusion of the injected ICG from the injection site was effectively prevented. In the laparoscopic operation, injection sites of the hydrogel in porcine stomach could be accurately detected in real time even after 3 days. This alginate hydrogel system may be potentially useful as an effective surgical marker in terms of accuracy and persistence for laparoscopic operation.

Re-assembled oleic acid-protein complexes as nano-vehicles for astaxanthin: Multispectral analysis and molecular docking

In the case of carotenoids, lipid delivery systems are superior in promoting intestinal absorption, while biopolymer-based delivery systems (e.g. protein) have advantages in biocompatibility, biodegradability and controlled release. Therefore, based on the multi-ligand binding properties of protein, we proposed fatty acid-protein complexes as nano-vehicles for encapsulating astaxanthin (ASTA). In this work, oleic acid (OA)–bovine serum albumin (BSA) complexes were fabricated by a pH-driven method. Under the optimized conditions, after OA binding to BSA at a molar ratio of 4:1, slight changes of protein secondary structure appeared and it's surface hydrophobicity increased from 14490 to 25324. When the binding molar ratios of ASTA to BSA ranged from 0.5:1 to 5:1, the ASTA–OA–BSA aqueous dispersions showed better clarity than that of ASTA–BSA. Compared with OA-free BSA, improved encapsulation efficiency and loading capacity were also observed for OA–loading BSA. Based on the fluorescence spectra and Stern–Volmer equation analysis, ASTA binding to the OA-loading BSA displayed a static manner mainly through hydrogen binding and van der Waals interactions. According to the results of site marker competitive experiments and molecular docking, the subdomains IIA and IIIA of BSA should be the acceptor sites of ASTA, and the subdomain IIIA was indicated to be the preferential one. Interestingly, OA as a protein ligand can dramatically enhanced the binding capacity of subdomain IIA to ASTA and make it the preferred acceptor site. In conclusion, OA–BSA nanoparticles as a delivery system should be suitable for fat-soluble nutrients such as carotenoids.

Formation of a bovine serum albumin diligand complex with rutin for the suppression of heme toxicity

Serum albumin binds avidly to heme to form heme–serum albumin complex and can protect against the potentially toxic effects of heme. Rutin is a glycoside of the bioflavonoid quercetin with various protective effects due to its antioxidant ability. Clarification of the interaction mechanisms between serum albumin and bioactive components (such as heme and flavonoid) is important to develop effective carriers for encapsulation of heme and suppression of its toxicity. In this study, bindings of bovine serum albumin (BSA) to heme and/or rutin were investigated by experimental and molecular docking techniques. The fluorescence of BSA was quenched by both heme and rutin in static mode (i.e. formation of BSA-monoligand complexes), which was confirmed by Stern-Volmer calculations. Although heme showed higher affinity to BSA than rutin, the interactions of both components with BSA did locate within subdomain IIA (site I). BSA-diligand complexes were successfully formed after the simultaneous addition of heme and rutin. Bioactive rutin in the BSA-diligand complex still kept strong free radical scavenging activity compared to free rutin or BSA-monoligand complex. Hydrogen peroxide (H2O2)-induced heme degradation and free iron release was inhibited upon BSA binding and further decreased in BSA-diligand complexes. Consistently, the cytotoxicity of heme and oxidative stress in endothelial cells was decreased in the BSA-diligand complexes relative to those of heme or BSA-heme complex, where the co-presence of rutin played an important role. These results suggest the possibility and advantage of developing BSA-based carriers for the suppression of heme toxicity in their biomedical applications.

Evaluation of competitive binding interaction of neratinib and tamoxifen to serum albumin in multidrug therapy.

Co-administration of two drugs to obtain a therapeutic goal is a common practice clinically and for effective use of drug therapy. However, the co-administration can sometimes cause adverse effects due to pharmacokinetic drug interactions. Breast Cancer treatment regimen include tyrosine kinase inhibitor neratinib (NRB) and/or tamoxifen (TMX). In this study neratinib and tamoxifen interaction with bovine serum albumin (BSA) and human serum albumin (HSA) individually and in combination using fluorescence spectroscopy was studied. The aim of this study was to find out whether there is a possibility of either of the two drugs interfering in the plasma protein binding of the other drug. Subdomain IIA of both the BSA and HSA was found to bind tamoxifen and neratinib. The λex = 280 nm and 295 nm were used for the analysis of neratinib-SA, tamoxifen-SA, neratinib: SA in presence of constant concentration of tamoxifen and similarly tamoxifen-SA in presence of constant concentration of neratinib. The interaction study of the binary and the ternary systems suggest that neratinib doesn't affect the interaction between SA and tamoxifen. In contrast, the interaction between neratinib and SA was affected by tamoxifen. The binding constant and quenching constant values suggest that tamoxifen dislodges neratinib from its serum albumin complex whereas neratinib doesn't affect the interaction between SA and tamoxifen. Thus, it was concluded from the results the study that during simultaneous administration of neratinib and tamoxifen, their competition for the SA binding sites should be taken into account.

Fungicide Tebuconazole Influences the Structure of Human Serum Albumin Molecule.

Studies of interactions between pesticides and target mammalian proteins are important steps toward understanding the pesticide′s toxicity. Using calorimetric and spectroscopic methods, the interaction between triazole fungicide tebuconazole and human serum albumin has been investigated. The spectroscopic techniques showed that fluorescence quenching of human serum albumin by tebuconazole was the result of the formation of tebuconazole/human serum albumin complex with the static type as the dominant mechanism. The association constant was found to be 8.51 × 103 L/mol. The thermodynamic parameters were obtained as ΔH = −56.964 kJ/mol, ΔS = −115.98 J/mol·K. The main active interactions forming the tebuconazole/human serum albumin complex were identified as the interplay between hydrogen bonds and/or van der Waals forces, based on thermodynamic experiments. These binding modes were corroborated well by the predictions of molecular modeling. Hydrogen bonding of tebuconazole with Arg222, Ala215 and Ala291 of human serum albumin played a relevant role in binding. The conformation changes in secondary structure were characterized by circular dichroism and 3D fluorescence spectra.

Effect of divalent cations on bovine serum albumin (BSA) and tannic acid interaction and its influence on turbidity and in vitro protein digestibility

Tannins, proteins, and divalent cations interactions are important for many processes in the food industry and human and animal nutrition and health. The effect of magnesium, calcium, and manganese on the interaction, turbidity, and in vitro protein digestibility of bovine serum albumin and tannic acid complexes was studied. The divalent cations increase the affinity and influence the enthalpy and entropy changes of the protein and tannin binding. Magnesium maintained the nature of interactions, and calcium and manganese changed the binding mechanism. The factor that most influenced turbidity was the tannic acid and divalent cations binary interaction. Samples containing tannic acid and magnesium and calcium decreased the protein digestibility. Manganese increased the in vitro protein digestibility when compared with samples without salt addition; nevertheless, the complexes formed was higher. These finds can help in the understanding of interactions involved food system and in physiological conditions.

Changes in cell differentiation and proliferation lead to production of abzymes in EAE mice treated with DNA-Histone complexes.

Experimental autoimmune encephalomyelitis (EAE)‐prone C57BL/6 mice are used as a model of human multiple sclerosis. We immunize mice with myelin oligodendrocyte glycoprotein (MOG), DNA–histone and DNA‐methylated bovine serum albumin (met‐BSA) complexes to reveal different characteristics of EAE development including bone marrow lymphocyte proliferation and differentiation profiles of hematopoietic stem cells. Immunization of C57BL/6 mice with MOG35‐55 results in the acceleration of EAE development. Anti‐DNA antibodies are usually directed against DNA–histone complexes resulting from cell apoptosis. During the acute EAE phase (7‐20 days after immunization), catalytic antibodies efficiently hydrolysing myelin basic protein (MBP), MOG and DNA are produced with parallel suppression of antibodies hydrolysing histones. We could show that in contrast to MOG, immunization with histone‐DNA results in a reduction of proteinuria, a significant increase in anti‐DNA, anti‐MBP and anti‐MOG antibody titres, as well as an increase in their catalytic activities for antigen hydrolysis, but slightly changes the concentration of cytokines. Contrary to MOG, DNA–histone and DNA‐met‐BSA only stimulated the formation of anti‐DNA antibodies hydrolysing DNA with a long delay (15‐20 days after immunization). Our data indicate that for C57BL/6 mice immunization with DNA‐met‐BSA and DNA–histone complexes may have opposing effects compared to MOG. DNA–histone stimulates the appearance of histone‐hydrolysing abzymes in the acute EAE phase, while abzymes with DNase activity appear at significantly later time‐points. We conclude that MOG, DNA–histone and DNA‐met‐BSA have different effects on numerous bone marrow, cellular, immunological and biochemical parameters of immunized mice, but all antigens finally significantly stimulate the development of the EAE.

Biomimetic Shells Endow Sub-50 nm Nanoparticles with Ultrahigh Paclitaxel Payloads for Specific and Robust Chemotherapy.

Poor loading capacity and nonspecific tumor accumulation of current drug delivery system remain the critical challenges that prevent nanomedicine from maximizing therapeutic efficacy in cancer treatment. Herein, poly(ester amide) polymers composed of cationic and hydrophobic segments were formulated with a paclitaxel/human serum albumin (PTX/HSA) complex, as well as free PTX, to construct a core-shell nanoparticle (NP) platform with the interior simultaneously reserving PTX and PTX/HSA complex, while the exterior absorbing the PTX/HSA complex. Following systematic screening, the optimized NPs, namely, APP1i@e NPs, exhibited small particle size (43.95 nm), maximal PTX loading (42.23%), excellent dynamic stability (at least 1 week), and acid-triggered release. In vitro results showed that after being trafficked through caveolae-mediated endocytosis, APP1i@e NPs successfully escaped from endo-/lysosomes and then rapidly released cargos in the acidic cytosol, which continued to enhance cytotoxicity by mitochondrial control of apoptosis and suppression of microtubule dynamics. Longer circulation time and superior targeting efficiency post-intravenous injection confirmed that surface PEGylation imparted APP1i@e NPs with the ability to control their pharmacokinetics and biodistribution. The biomimetic shell design with HSA, which enlarged PTX stock and improved biosafety, made APP1i@e NPs more suitable for in vivo applications. Furthermore, in vivo safety and efficacy demonstrated that APP1i@e NPs effectively inhibited the growth of ovarian xenograft tumors, whereas significantly avoiding toxic issues associated with PTX. APP1i@e NPs with surface PEG coating and biomimetic HSA design, therefore, may provide a remarkable improvement in the therapeutic index of taxanes used in the clinic.

Generation of a Diligand Complex of Bovine Serum Albumin with Quercetin and Carbon Nanotubes for the Protection of Bioactive Quercetin and Reduction of Cytotoxicity.

The interactions between proteins and bioactive ligands (such as flavonoids and nanomaterials) are vital to the design of effective protein carriers for the protection of bioactive molecules and reduction of the cytotoxicity of nanotubes. Bovine serum albumin (BSA) can bind various bioactive components and subsequently form protein-ligand complexes. Herein, the binding of BSA to quercetin and single-walled carbon nanotubes (SWCNTs) was investigated by using experimental and molecular-docking methods. The fluorescence intensity of BSA was decreased by both quercetin and SWCNTs in static quenching mode (i.e., compound formation), which was authenticated by Stern-Volmer calculations. Although quercetin showed a higher affinity for BSA than SWCNTs, the binding of both components to BSA was located in site I (subdomain IIA). BSA-diligand complexes were successfully generated when SWCNTs and quercetin, in that sequence, were added. The cytotoxicity of SWCNTs and the formation of reactive oxygen species in endothelial cells were decreased with the BSA-diligand complexes relative to those of SWCNTs or BSA-SWCNT corona, whereas the stability problems of quercetin were ameliorated in the BSA-diligand complex relative to in the free flavonoid. The BSA-diligand complex showed a better inhibitive effect on the cytotoxicity of SWCNTs than the BSA-SWCNT complex, and thus the coexistence of quercetin played a crucial role. These data demonstrate the advantages and possibility of designing BSA carriers for the protection of bioactive ligands and reduction of the cytotoxicity of nanotubes in functional-food and biomedical applications.

Synthesis and characterization of binary complexes of furcellaran with gelatin and bovine serum albumin

Furcellaran (FUR) complexes with albumin (BSA) and gelatin (GEL) were investigated. The zeta potential (ζ) values of furcellaran, gelatin and their mixtures at weight ratios 2 : 1, 1 : 1, and 1 : 2 (w/w) were measured over a pH range 2.0–10.0. FUR/GEL and FUR/BSA complexes were prepared by the electrolysis of aqueous solutions of both components taken in the 1 : 1 (w/w) ratio. The results of the elemental analysis, FT-IR spectroscopy and thermal analysis confirmed the formation of the complexes. The investigated complexes differed in their susceptibility to enzymatic hydrolysis and solubility. At room temperature, the solubility of FUR/GEL and FUR/BSA complexes was 0.055 ± 0.021 g/100 cm3 H2O and 0.031 ± 0.020 g/100 cm3 H2O, respectively. Different structures of FUR/GEL and FUR/BSA complexes, determined by SEM studies, can explain differences in both solubility and hydrolytic susceptibility. Enzymatic studies showed that the furcellaran/gelatin and furcellaran/bovine serum albumin complexes are biodegradable. The complexes were not physical mixtures of the components.

Probing the binding of Spathodea campanulata leaves extract mediated biogenic potential microbicidal silver nanoparticles to human serum albumin: An insight in the light of spectroscopic approach

Nanomaterials are used to modify and improve the pharmacodynamic and pharmacokinetic properties of drug molecules of diverse types. The plant extracts are safe, beneficial and ecological for the synthesis of the large scale of nanomaterials. Herein, we report the new ultra fast silver nanoparticles (SNPs) synthesis via green route using aqueous Spathodea campanulata leaf extracts without using any external reducing ̸ stabilizing agent and assessment of their bio-logical application. The maximum UV–Vis spectroscopic absorbance was observed at 438 nm. EDX spectra also confirmed the construction of SNPs. TEM analysis revealed that the biogenic SNPs were of 18.4 nm in size (d). Hydrodynamic size (d = ~20 nm) was deliberated by the DLS. FT-IR study indicated that OH, NH, N-O, CO and COOH functional groups participated in the construction of SNPs. The zeta potential value (−16.8 mV) confirmed the dispersion and stability of the SNPs. The SNPs showed a dose dependent bactericidal property against Escherichia coli ATCC 25922 and MIC was found to be 1.2 nM for it. The binding of SNPs with human serum albumin (HSA) and SNPs-HSA complex were investigated by UV–Vis absorbance, fluorescence, circular dichroism (CD) spectroscopy, fluorescence lifetime and zeta potential measurement. The slight conformational changes of the protein in the presence of SNPs were confirmed by absorbance, 3D fluorescence, synchronous fluorescence and CD spectroscopy. This work improves our knowledge about the structural nature of binding between the biogenic SNPs and HSA.

Gold nanoparticles as a factor of influence on doxorubicin–bovine serum albumin complex

The interaction between doxorubicin (Dox) and bovine serum albumin (BSA) complex with gold nanoparticles (AuNPs) was investigated by optical spectroscopy. The optical absorption of Dox and BSA solutions was studied. The formation of Dox–BSA complexes with a binding constant K = 7.56 × 106 M−2 and the number of binding sites n = 2 was found out. With pH 6.9, the concentration of complexes is an order of magnitude lower than the concentration of unbound antibiotic molecules. Optical absorption in solutions of Dox–BSA conjugates in the presence of AuNPs undergoes a significant rearrangement, which manifests the changes in the magnitude of the hydrophobic interaction of BSA with Dox, changes in the conformational state of antibiotic, and, as a consequence, a plasmon-induced change in the mechanism of complex formation. The aggregation of the Dox–AuNPs conjugate depends on the presence and concentration of BSA and in the case of formation of the Dox–BSA complex is minimal.