Interaction of pirenzepine with bovine serum albumin and effect of β-cyclodextrin on binding: A biophysical and molecular docking approach

Rahman, Yusra; Afrin, Shumaila; Tabish, Mohammad

doi:10.1016/j.abb.2018.06.005

Cited by 38 publications

(15 citation statements)

References 22 publications

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“…Molecular docking analyses showed that BrNs has strong interactions with binding score of −8.08 kcal/mol using swissdock, and −231.64 kJ/mol using Hex 8.0 on the basis of shape and electrostatics parameters. The experimentally derived value for binding energy was −5.1 kcal/mol at 298 K and is closely related to the theoretically derived value 52 , 53 . BrNs was found to have strong binding to alpha helices domain with hydrophobic interactions at Arg208, Ala212, Ala246, Leu346 and Ala349 residues and one hydrogen bond of bond length 3.09 angstroms with Lys350 residue and pi-cation interaction with Arg208 of distance 4.15 angstroms of BSA protein (Fig.…”

Section: Resultssupporting

confidence: 80%

Mechanistic Interaction Study of Bromo-Noscapine with Bovine Serum Albumin employing Spectroscopic and Chemoinformatics Approaches

Sood

Kumar

Rathee

et al. 2018

Sci Rep

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Bromo-Noscapine (BrNs) is a tubulin-binding cytotoxic agent with significant activity against breast and lung cancer. The mechanistic interaction insight into the binding of bovine serum albumin (BSA) with BrNs can provide critical information about the pharmacodynamics and pharmacokinetics properties. Here, various spectroscopic techniques and computational methods were employed to understand the dynamics of BrNs and BSA interaction. The intrinsic fluorescence of BSA was quenched by BrNs through a static quenching procedure. The stoichiometry of BrNs-BSA complex was 1:1 and binding constant of the complex was in the order of 103 M−1 at 298 K. Based on thermodynamic analysis, it was deduced that binding process of the BrNs with BSA was spontaneous and exothermic, and the major forces between BrNs and BSA were van der waals forces and hydrogen bonding. Moreover, results of FT-IR, CD, UV spectra concluded significant conformational change in BSA on binding with BrNs. The in vitro findings were further confirmed by in silico assays. Molecular docking showed strong interactions with score of −8.08 kcal/mol. Molecular dynamics simulation analysis also suggested the stable binding with lower deviation in RMSD and RMSF values through persistent long simulation run. This study suggests optimal efficiency of diffusion of the BrNs into the bloodstream for the treatment of cancer.

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Section: Resultssupporting

confidence: 80%

Mechanistic Interaction Study of Bromo-Noscapine with Bovine Serum Albumin employing Spectroscopic and Chemoinformatics Approaches

Sood

Kumar

Rathee

et al. 2018

Sci Rep

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“…Fluorescence emission spectra of RPG-BSA system were recorded at 298 K in the presence and absence of Cu 2+ and Zn 2+ ions, separately. For this, the concentration of BSA and metal ion was kept constant (1.67 μM) whereas that of RPG was varied from 1.67 to 15.0 μM [11,12].…”

Section: Methodsmentioning

confidence: 99%

Interaction of repaglinide with bovine serum albumin: Spectroscopic and molecular docking approaches

Pawar

Seetharamappa

2019

Journal of Pharmaceutical Analysis

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Repaglinide (RPG) regulates the amount of glucose by stimulating the pancreas to release insulin in the blood. In view of its biological importance, we have examined the interaction between RPG and a model protein, bovine serum albumin (BSA) employing various spectroscopic, electrochemical and molecular docking methods. Fluorescence spectra of BSA were recorded in the presence and absence of RPG in phosphate buffer of pH 7.4. Fluorescence intensity of BSA was decreased upon the addition of increased concentrations of RPG, indicating the interaction between RPG and BSA. Stern-Volmer quenching analysis results revealed that RPG quenched the intensity of BSA through dynamic quenching mechanism. This was further confirmed from the time-resolved fluorescence measurements. The binding constant as calculated from the spectroscopic and voltammetric results was observed to be in the order of 10 4 M −1 at 298 K, suggesting the moderate binding affinity between RPG and BSA. Competitive experimental results revealed that the primary binding site for RPG on BSA was site II. Absorption and circular dichroism studies indicated the changes in the secondary structure of BSA upon its interaction with RPG. Molecular simulation studies pointed out that RPG was bound to BSA in the hydrophobic pocket of site II.

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“…In other words, the unfavorable positive enthalpy change (ΔH° = 5.13 ± 0.29 kJ mol -1 ) is compensated by the positive entropy change (ΔS° = 0.117 ± 0.001 kJ mol -1 K -1 ), suggesting that the binding of 4c to HSA may be governed by desolvation and/or hydrophobic factors. 59 In addition, according to the Ross and Subramanian 60 theory, hydrogen bonding can also be considered as the main binding force due to ΔH° > 0.…”

Section: Scheme 2 Preparation Of Novel Modifiedmentioning

confidence: 99%

“…These theoretical results are in full accordance with the intermolecular interactions suggested by the experimental thermodynamic parameters described above. 59…”

Section: Competitive Binding Studies and Theoretical Analysis On Hsa:4cmentioning

confidence: 99%

Design, Synthesis, Trypanocidal Activity, and Studies on Human Albumin Interaction of Novel S-Alkyl-1,2,4-triazoles

Franklim¹,

Freire-de-Lima²,

Chaves³

et al. 2019

J. Braz. Chem. Soc.

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Chagas disease is a neglected tropical disease caused by the hemoflagellated parasite Trypanosoma cruzi (Kinetoplastida). The only available drug to treat chagasic patients in Brazil, the nitroheterocycle benznidazole, is effective solely during the acute phase of the infection. There is accordingly a need to develop new therapeutic tools for the treatment of Chagas disease. This work reports the synthesis, trypanocidal evaluation and human serum albumin (HSA) interactions of a novel series of 1,2,4-triazoles. The new derivatives were synthesized via microwave irradiation in good yields. Most compounds showed toxic effects against T. cruzi with low toxicity to host cells. Three S-alkylated-triazoles showed the best activity profile against amastigotes, with half maximal inhibitory concentration (IC 50) values of 3.95 ± 1.41, 4.15 ± 0.92 and 3.61 ± 0.65 μmol L-1 , respectively. The interaction between HSA and 3-[(1E,3E)-4-(1,3-benzodioxol-5-yl)buta-1,3-dien-1-yl]-5-(butylthio)-4-cyclohexyl-4,5-dihydro-1H-1,2,4-triazole was investigated using multiple spectroscopic techniques and molecular docking, revealing that serum albumin is a potential endogenous carrier to this compound in the human bloodstream.

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Interaction of pirenzepine with bovine serum albumin and effect of β-cyclodextrin on binding: A biophysical and molecular docking approach

Cited by 38 publications

References 22 publications

Mechanistic Interaction Study of Bromo-Noscapine with Bovine Serum Albumin employing Spectroscopic and Chemoinformatics Approaches

Mechanistic Interaction Study of Bromo-Noscapine with Bovine Serum Albumin employing Spectroscopic and Chemoinformatics Approaches

Interaction of repaglinide with bovine serum albumin: Spectroscopic and molecular docking approaches

Design, Synthesis, Trypanocidal Activity, and Studies on Human Albumin Interaction of Novel S-Alkyl-1,2,4-triazoles

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