scholarly journals Investigating the Size-Dependent Binding of Pristine nC60 to Bovine Serum Albumin by Multi-Spectroscopic Techniques

Materials ◽  
2021 ◽  
Vol 14 (2) ◽  
pp. 298
Author(s):  
Shufang Liu ◽  
Shu’e Wang ◽  
Zhanzuo Liu
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Constants ◽  
Inner Filter Effect ◽  
Spectroscopic Techniques ◽  
Size Distributions ◽  
Size Dependent ◽  
Filter Effect ◽  
Vis Spectroscopy

The morphology of nanomaterials may affect their interaction with biomacromolecules such as proteins. Previous work has studied the size-dependent binding of pristine nC60 to bovine/human serum albumin using the fluorometric method and found that the fluorescence inner filter effect might affect this interaction. However, if it is necessary to accurately calculate and obtain binding information, the fluorescence inner filter effect should not be ignored. This work aimed to further investigate the effect of the fluorescence inner filter on the interaction between pristine nC60 with different particle sizes (140–160, 120–140, 90–110, 50–70, and 30–50 nm) and bovine serum albumin for a more accurate comprehension of the binding of pristine nC60 to bovine serum albumin. The nC60 nanoparticles with different size distributions used in the experiments were obtained by the solvent displacement and centrifugation method. UV-Vis spectroscopy and fluorescence spectroscopy were used to study the binding of nC60 with different size distributions to bovine serum albumin (BSA) before and after eliminating the fluorescence inner filter effect. The results showed that the fluorescence inner filter effect had an influence on the interaction between nC60 and proteins to some extent, and still did not change the rule of the size-dependent binding of nC60 nanoparticles to BSA. Further studies on the binding parameters (binding constants and the number of binding sites) between them were performed, and the effect of the binding on BSA structures and conformation were also speculated.

Ratiometric fluorescence determination of alkaline phosphatase activity based on dual emission of bovine serum albumin-stabilized gold nanoclusters and the inner filter effect

The Analyst ◽  
2021 ◽  
Author(s):  
Li Pu ◽  
Mengfan Xia ◽  
Pengyue Sun ◽  
Yaodong Zhang
Keyword(s):  
Alkaline Phosphatase ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Gold Nanoclusters ◽  
Inner Filter Effect ◽  
Ratiometric Fluorescence ◽  
Dual Emission ◽  
Filter Effect

Ratiometric fluorescence assay of alkaline phosphatase based on dual emission of bovine serum albumin-templated gold nanoclusters and inner filter effect.

scholarly journals Study on the interaction between ketoprofen and bovine serum albumin by molecular simulation and spectroscopic methods

2011 ◽  
Vol 26 (6) ◽  
pp. 337-348 ◽  
Author(s):  
Jin Lian Zhu ◽  
Jia He ◽  
Hua He ◽  
Shu Hua Tan ◽  
Xiao Mei He ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Molecular Simulation ◽  
Bovine Serum ◽  
Binding Constants ◽  
Simulation Method ◽  
Binding Mode ◽  
Tryptophan Residue ◽  
Vis Spectroscopy ◽  
Static And Dynamic Quenching

The interaction between ketoprofen and bovine serum albumin (BSA) was investigated by molecular simulation, fluorescence and UV-vis spectroscopy methods under the simulated physiological conditions. Molecular simulation method performed to reveal the possible binding mode or mechanism suggested the binding forces between ketoprofen and BSA were mainly hydrophobic interaction and hydrogen bond, which was in agreement with the thermodynamic study (ΔHΦand ΔSΦwere calculated to be 74.514 kJ/mol and 333.98 J/mol · K). The binding constants of ketoprofen and BSA at different temperatures (298, 310 and 318 K) were calculated according to the data obtained from fluorescence spectra and the results indicated that ketoprofen had strong ability to quench the intrinsic fluorescence of BSA via a combination of static and dynamic quenching. Meanwhile, the changes of the conformation of BSA caused by ketoprofen were qualitatively analyzed with the UV-vis and synchronous fluorescence spectroscopy. The distance between ketoprofen and tryptophan residue in BSA was calculated to be 1.58 nm.

Exploration of Fungal Lipase as Direct Target of Eugenol through Spectroscopic Techniques

2019 ◽  
Vol 26 (12) ◽  
pp. 919-929
Author(s):  
Farheen Naz ◽  
Haider Anis ◽  
Ziaul Hasan ◽  
Asimul Islam ◽  
Luqman A. Khan
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Sites ◽  
Bovine Serum ◽  
Structural Changes ◽  
Tertiary Structure ◽  
Spectroscopic Techniques ◽  
Vis Spectroscopy ◽  
Direct Target

Background:Fungal lipase dependent processes are important for their pathogenicity. Lipases can therefore be explored as direct target of promising herbal antifungals.Objective:We explored Aspergillus niger lipase as a direct target of eugenol through spectroscopic techniques and compare results with Bovine Serum Albumin and lysozyme to comment on selectivity of eugenol towards lipase.Methods:In vitro activity assays of lipase are used to determine concentration ranges. UV-Visible, Fluorescence and Circular dichroism spectroscopy were employed to determine binding constant, stoichiometric binding sites and structural changes in Lipase, BSA and lysozyme following incubation with varying concentrations of eugenol.Results:In activity assays 50% inhibition of lipase was obtained at 0.913 mmoles/litre eugenol. UV-vis spectroscopy shows formation of lipase-eugenol, Bovine Serum Albumin-eugenol and lysozyme-eugenol complex well below this concentration of eugenol. Eugenol binding caused blue shift with Bovine Serum Albumin and lysozyme suggestive of compaction, and red shift with lipase. Negative ellipticity decreased with lipase but increased with Bovine Serum Albumineugenol and lysozyme-eugenol complexes suggesting loss of helical structure for lipase and compaction for Bovine Serum Albumin and lysozyme. Binding of eugenol to lipase was strong (Ka= 4.7 x 106 M-1) as compared to Bovine Serum Albumin and lysozyme. The number of stoichiometric eugenol binding sites on lipase was found to be 2 as compared to 1.37 (Bovine Serum Albumin) and 0.32 (lysozyme). Docking results also suggest strong binding of eugenol with lipase followed by Bovine Serum Albumin and lysozyme.Conclusion:Eugenol is found to be effective inhibitor and disruptor of secondary and tertiary structure of lipase, whereas its binding to Bovine Serum Albumin and lysozyme is found to be weak and less disruptive of structures suggesting selectivity of eugenol towards lipase.

Bovine serum albumin-capped CdS quantum dots as an inner-filter effect sensor for rapid detection and quantification of protamine and heparin

2015 ◽  
Vol 7 (19) ◽  
pp. 8445-8452 ◽  
Author(s):  
Hongxia Li ◽  
Xiaohong Yang
Keyword(s):  
Quantum Dots ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Rapid Detection ◽  
Inner Filter Effect ◽  
Cds Quantum Dots ◽  
Filter Effect ◽  
Sensitive Sensor ◽  
Detection And Quantification

In this work, we developed a novel and sensitive sensor for the detection of heparin and protamine based on the inner-filter effect (IFE) between gold nanoparticles (AuNPs) and bovine serum albumin-capped CdS quantum dots (QDs).

Static and Dynamic Aspects of Supramolecular Interactions of Coumarin 153 and Fluorescein with Bovine Serum Albumin

2012 ◽  
Vol 65 (9) ◽  
pp. 1305 ◽  
Author(s):  
Rajeev Yadav ◽  
Shyamashis Das ◽  
Pratik Sen
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Resonance Energy ◽  
Binding Constants ◽  
Docking Study ◽  
Supramolecular Interactions ◽  
Spectroscopic Techniques ◽  
Molecular Docking Study ◽  
Coumarin 153

The static and dynamic aspects of supramolecular interactions between coumarin 153 (C153) and fluorescein (FL) with bovine serum albumin (BSA) has been studied by spectroscopic techniques. Both dyes were found to form 1 : 1 complexes with BSA, with binding constants 2.9 ± 0.3 × 105 M–1 and 2.1 ± 0.2 × 105 M–1 for C153 and FL respectively. The binding site of C153 has been determined by steady-state fluorescence resonance energy transfer, site marker competitive experiments, and a molecular docking study. Our studies indicate that C153 binds to domain IIIA of BSA whereas FL binds non-specifically. Denaturation characteristics of the C153 and FL binding region of BSA were found to be very different to global denaturation. Furthermore, kinetics of binding has been studied by the stopped-flow method. The observed rate constants were found to be 8.8 s–1 and 5.9 s–1 for C153 and FL respectively.

scholarly journals Effect of Moderate UVC Irradiation on Bovine Serum Albumin and Complex with Antimetabolite 5-Fluorouracil: Fluorescence Spectroscopic and Molecular Modelling Studies

2015 ◽  
Vol 2015 ◽  
pp. 1-12 ◽  
Author(s):  
Shanmugavel Chinnathambi ◽  
Subramani Karthikeyan ◽  
Devadasan Velmurugan ◽  
Nobutaka Hanagata ◽  
Prakasarao Aruna ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Molecular Modelling ◽  
Bovine Serum ◽  
Spectroscopic Techniques ◽  
Time Resolved ◽  
Vis Spectroscopy ◽  
Molecular Modelling Studies ◽  
Modelling Studies ◽  
The Stability

The interaction of antimetabolite 5-fluorouracil (5FU) with bovine serum albumin (BSA) under UVC (253.7 nm) irradiation was investigated in the present study using UV-Vis spectroscopy, steady state/time resolved fluorescence spectroscopic techniques. The stability of protein was found to be very strong when BSA gets bind to 5FU and moreover it is compared with the free BSA under UVC irradiation. From the fluorescence spectroscopic study, the stability of the complex was found to acquire 2-fold stronger than free protein. From the molecular modelling studies, we came to know the hydrogen bonds between BSA and antimetabolite 5FU are strong, up to 70.4 J/m2 under UVC irradiation.

Box-Behnken Design Optimized TPGS Coated Bovine Serum Albumin Nanoparticles Loaded with Anastrozole

2021 ◽  
Vol 18 ◽  
Author(s):  
Ashish Kumar ◽  
Ajit Singh ◽  
S.J.S Flora ◽  
Rahul Shukla
Keyword(s):  
Particle Size ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Glycol Succinate ◽  
Burst Release ◽  
Spectroscopic Techniques ◽  
Potential Candidate ◽  
Box Behnken Design ◽  
Thermal Gelation

Purpose: In this study, a novel D-α-tocopheryl polyethylene glycol succinate (TPGS) modified bovine serum albumin (BSA) nanoparticles were developed for delivery of Anastrozole (ANZ) which is optimized by Box-Behnken design (BBD). This TPGS-ANZ-BSA NPs are evaluated for their physicochemical and drug release characteristics. Methods: TPGS-ANZ-BSA NPs were prepared by desolvation thermal gelation method andthe effects of critical process parameter (CPP)which are BSA amount, TPGS concentration and stirring speed on the critical quality attributes (CQA) such as % drug loading (%DL) and particle size were studied using BBD. TPGS-ANZ-BSA NPs were characterized using different spectroscopic techniques including UV-Visible and FTIR is used to confirm the entrapment of ANZ in BSA. DSC and PXRD revealed the amorphization of ANZ in the TPGS-ANZ-BSA NPs after freeze drying. Scanning electron microscopy (SEM) analysis was performed for the surface morphologyanalysesNPs. In vitro release studies were performed at pH 5.5 and pH 7.4 for 48h to mimic tumour microenvironment. Results: The BBD optimized batch showed 107 nm particle size with % DL of 8.5± 0.5 of TPGS-ANZ-BSA NPs. The spectroscopic and thermal characterizations revealed the successful encapsulation of ANZ inside the nanoparticles.The TPGS-ANZ-BSA NPs were found to exhibit burst release at pH 5.5 and sustained release at pH 7.4. The short-term stability of drug-loaded nanoparticles displayed no significant changes in physicochemical properties at room temperature for period of one month. Conclusion: The BBD optimized TPGS-ANZ-BSA nanoparticles showed enhanced physiochemical properties for ANZ and potential candidate for anticancer agent drugs delivery.

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