Evaluation of the interaction of levothyroxine with bovine serum albumin using spectroscopic and molecular docking studies

Sandu, Nicoleta; Chilom, Claudia G.; David, Melinda; Florescu, Monica

doi:10.1080/07391102.2020.1822919

Cited by 21 publications

(5 citation statements)

References 40 publications

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“…For this reason, the evaluation of the optical measurements was re-assessed based on the Scatchard plot (Equation (3)), which is a special methodology for protein/small molecule or protein/small particle interactions [ 51 ]:

where the F 0 and F are the emission intensities at 350 nm before and after the addition of NCs, respectively, K a is the binding constant, N is the number of binding sites of BSA to the cluster, and [ Q ] is the applied NC concentration [ 52 ].…”

Section: Resultsmentioning

confidence: 99%

Promising Bioactivity of Vitamin B1-Au Nanocluster: Structure, Enhanced Antioxidant Behavior, and Serum Protein Interaction

et al. 2023

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In the current work, we first present a simple synthesis method for the preparation of novel Vitamin-B1-stabilized few-atomic gold nanoclusters with few atomic layers. The formed nanostructure contains ca. eight Au atoms and shows intensive blue emissions at 450 nm. The absolute quantum yield is 3%. The average lifetime is in the nanosecond range and three main components are separated and assigned to the metal–metal and ligand–metal charge transfers. Based on the structural characterization, the formed clusters contain Au in zero oxidation state, and Vitamin B1 stabilizes the metal cores via the coordination of pyrimidine-N. The antioxidant property of the Au nanoclusters is more prominent than that of the pure Vitamin B1, which is confirmed by two different colorimetric assays. For the investigation into their potential bioactivity, interactions with bovine serum albumin were carried out and quantified. The determined stoichiometry indicates a self-catalyzed binding, which is almost the same value based on the fluorometric and calorimetric measurements. The calculated thermodynamic parameters verify the spontaneous bond of the clusters along the protein chain by hydrogen bonds and electrostatic interactions.

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Section: Resultsmentioning

confidence: 99%

Promising Bioactivity of Vitamin B1-Au Nanocluster: Structure, Enhanced Antioxidant Behavior, and Serum Protein Interaction

et al. 2023

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“…FDA and FD donate the strength of BSA's tryptophan residue emission with or without R1 ; K 2 represents the dipole alignment that is assumed to be 2/3 for fluid solutions; ϕ D represents the quantum yield of donor molecule; η = 1.335 (refractive index); in the following equation, J represents the integral of the overlap between the absorption‐emission outcome of the acceptor–donor sites. [ 71,72 ]

J goodbreak= \frac{\int_{0}^{\infty} F ((), λ) ϵ ((), λ) λ^{4} d ((), λ)}{\int_{0}^{\infty} F ((), λ) d ((), λ)} .

…”

Section: Resultsmentioning

confidence: 99%

Mixed ligand approach for novel hydrazide copper(II) complexes: Structural aspects, theoretical investigation and their biological evaluation

Richa

Kiran

Kushwaha

et al. 2023

Applied Organom Chemis

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In this paper, two novel Cu(II) complexes [CuL(S-1-amino-2-propanol)] (R1) and [CuL(S-2-amino-1-propanol)] (R2) have been synthesized and characterized using Fourier transform infrared (FT-IR), thermogravimetric analysis (TGA), high-resolution mass spectrometry (HR-MS), scanning electron microscopy (SEM) and single crystal X-ray diffraction (SCXRD) technique.The single-crystal XRD analyses show that compounds R1 and R2 crystallized in triclinic and monoclinic crystal systems with P-1 and P2 1 space groups, respectively. The τ5 parameter values of R1 and R2 confirmed distorted square pyramidal geometry around Cu(II) centre. The compounds R1 and R2 possess 2D polymeric chains with (4,4)IIIa and 2C1 topology, respectively. The non-covalent interactions and electrostatic properties were investigated using Hirshfeld surface analysis and density functional theory (DFT). DFT calculations revealed higher stability of R1 over R2. The presence of strong hyper conjugative interactions in carbon-carbon and carbonnitrogen bonds has been confirmed by natural bond orbital (NBO) analysis. Time-dependent (TD)-DFT calculations were also performed to determine the excited state properties. Based on theoretical calculations, the simulated spectra showed absorption maxima at 506 and 743 nm for both complexes. Antimicrobial assays revealed that R1 is significantly antimicrobial against Pseudomonas aeruginosa at 512 and 256 μg/mL for Staphylococcus aureus, correspondingly. Serum binding studies of R1 confirm the existence of instinctive bonding interactions due to negative values on account of ΔG, ΔS and ΔH obtained from thermodynamics studies. In silico molecular dynamics and docking approaches have been used to validate the experimental findings of anti-microbial assay and serum binding studies. A high dock score for R1 over R2 revealed the high binding energy of the former with bacterial protein. It was found that the protein-ligand complex remained stable throughout the dynamic simulation process, and substantial interactions between R1 and bovine serum albumin were observed.

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“…There have been many investigations in the drug-serum albumin binding in recent years (60). The interactions of levothyroxine (61), resveratrol (62), diazepam, warfarin, phenylbutazone, iodipamide, azapropazone, tolbutamide, iophenoxic acid, indomethacin, furosemide, bucolome, sulfisoxazole, diclofenac and more drugs with albumin have been analyzed by several methods (45). Kurkov et al (58) showed the in vitro binding behavior of AZA on HSA.…”

Section: Discussionmentioning

confidence: 99%

Surface Plasmon Resonance Binding Study on the Interaction of Acetazolamide and Bovine Serum Albumin

TÜRKOĞLU,

AYDIN

2023

Clinical and Experimental Health Sciences

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Objective: Serum albumins are major plasma proteins in systemic blood circulation and act as transport proteins for endogenous and exogenous compounds such as drugs. In pharmaceutical applications, it is essential to characterize how drugs bind to serum albumin in the evaluation of drug candidates. Surface plasmon resonance (SPR) is fast, real-time, label-free optical based detection technique that offers the monitoring of molecular interactions, analyzing binding reactions and determining the affinity constants with real-time and high sensitivity. Acetazolamide (AZA) is used in the treatment of epilepsy and glaucoma. Methods: To determine the binding kinetics of AZA-Bovine serum albumin (BSA) interaction, (i) SPR gold sensor surface was functionalized, (ii) amine coupling procedure was applied to activate the surface group and BSA was immobilized on functionalized sensor surface, (iii) the concentration series of AZA (10, 25, 50, 75, 100, 150, 200 and 250 µM) was injected to SPR system and (iv) kinetic values were measured using the software of SPR system. Results: 5 mM MUA was coated for surface functionalization. 250 µg/mL BSA as ligand, 30 µL/min flow rate, 1X PBS buffer (pH 7.4) and 10 mM acetate buffer (pH 5.2) as running and coupling buffers, respectively, were performed for SPR binding study. According to result, equilibrium constant (KD) of AZA-BSA was determined as 67.72 µM. Conclusion: In this study, we investigated the AZA-BSA binding interaction using SPR system based on Kretchmann configuration. The study designed with fast, label-free and real-time approach will provide valuable knowledge for pharmaceutical and clinical applications.

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Evaluation of the interaction of levothyroxine with bovine serum albumin using spectroscopic and molecular docking studies

Cited by 21 publications

References 40 publications

Promising Bioactivity of Vitamin B1-Au Nanocluster: Structure, Enhanced Antioxidant Behavior, and Serum Protein Interaction

Promising Bioactivity of Vitamin B1-Au Nanocluster: Structure, Enhanced Antioxidant Behavior, and Serum Protein Interaction

Mixed ligand approach for novel hydrazide copper(II) complexes: Structural aspects, theoretical investigation and their biological evaluation

Surface Plasmon Resonance Binding Study on the Interaction of Acetazolamide and Bovine Serum Albumin

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