Hydrogen bonding-assisted interaction between amitriptyline hydrochloride and hemoglobin: spectroscopic and molecular dynamics studies

Maurya, Neha; Maurya, Jitendra Kumar; Kumari, Meena; Khan, Abbul Bashar; Dohare, Ravins; Patel, Rajan

doi:10.1080/07391102.2016.1184184

Cited by 36 publications

(33 citation statements)

References 80 publications

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“…The k q for 4MMC‐BSA complex is calculated as 5.5 × 10 11 (L mol −1 s −1 ), which is higher than known maximum collision rate constant (2 × 10 10 L mol −1 s −10 ) . This result again confirms static quenching mechanism resulting from ground state complex formation between 4MMC and BSA …”

Section: Resultssupporting

confidence: 59%

Esterase activity and conformational changes of bovine serum albumin toward interaction with mephedrone: Spectroscopic and computational studies

Patel

Maurya

Parray

et al. 2018

J of Molecular Recognition

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The present work is a brief overview of the effect of psychostimulant drug mephedrone hydrochloride (4MMC) on a transport protein, bovine serum albumin (BSA). The binding effect of 4MMC on BSA has been investigated by using UV-visible, steady-state fluorescence, time-resolved fluorescence, fluorescence resonance energy transfer, Fourier transform infrared, circular dichroism, and molecular docking method. 4-Methylmephedrone quenched the intrinsic fluorescence of BSA by static quenching mechanism, which was further confirmed by time-resolved fluorescence. The absorption spectrum of BSA in the presence of various concentrations of 4MMC reveals the change in the absorption bands of BSA-4MMC complex. The binding constant between 4MMC and BSA was calculated to be of the order of 10 Lmol . The thermodynamic parameters such as molar enthalpy change (∆H), molar Gibbs free energy change (∆G), and molar entropy contribution (∆S) were obtained by the van't Hoff equation. The values obtained suggested that the binding mechanism was entropic driven and the major forces involved are hydrophobic in nature. The fluorescence resonance energy transfer result indicates the high probability of energy transfer from Trp residue of BSA to the 4MMC (r = 2.01 nm). Fourier transform infrared and CD results showed that 4MMC induced secondary structural changes in BSA. The esterase-like activity of BSA in presence of 4MMC further validated our CD results, confirming the distortion and change in functionality of protein upon binding with 4MMC. Molecular docking analysis showed that 4MMC principally bind at the II site (subdomain IIIA) of BSA.

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Section: Resultssupporting

confidence: 59%

Esterase activity and conformational changes of bovine serum albumin toward interaction with mephedrone: Spectroscopic and computational studies

Patel

Maurya

Parray

et al. 2018

J of Molecular Recognition

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“…18 In addition, HHb plays an exceptional role in not only a buffering action 18 for oxygen, but also acts as a potential agent in the transport of a number of drugs to their targeted tissues. 19,20 To further investigate the side effects of CNPs in the bloodstream, lymphocyte cell viability was explored to examine the effects of CNPs on the basic immunological functions of human lymphocytes.…”

Section: Introductionmentioning

confidence: 99%

Biophysical, docking, and cellular studies on the effects of cerium oxide nanoparticles on blood components: in vitro

Eskandari¹,

Babadaei²,

Nikpur³

et al. 2018

IJN

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IntroductionThe application of nanoparticles (NPs) in medicine and biology has received great interest due to their novel features. However, their adverse effects on the biological system are not well understood.Materials and methodsThis study aims to evaluate the effect of cerium oxide nanoparticles (CNPs) on conformational changes of human hemoglobin (HHb) and lymphocytes by different spectroscopic (intrinsic and synchronous fluorescence spectroscopy and far and near circular dichroism [CD] spectroscopy), docking and cellular (MTT and flow cytometry) investigations.Results and discussionTransmission electron microscopy (TEM) showed that CNP diameter is ~30 nm. The infrared spectrum demonstrated a strong band around 783 cm−1 corresponding to the CNP stretching bond. Fluorescence data revealed that the CNP is able to quench the intrinsic fluorescence of HHb through both dynamic and static quenching mechanisms. The binding constant (Kb), number of binding sites (n), and thermodynamic parameters over three different temperatures indicated that hydrophobic interactions might play a considerable role in the interaction of CNPs with HHb. Synchronous fluorescence spectroscopy indicated that microenvironmental changes around Trp and Tyr residues remain almost unchanged. CD studies displayed that the regular secondary structure of HHb had no significant changes; however, the quaternary structure of protein is subjected to marginal structural changes. Docking studies showed the larger CNP cluster is more oriented toward experimental data, compared with smaller counterparts. Cellular assays revealed that CNP, at high concentrations (>50 µg/mL), initiated an antiproliferative response through apoptosis induction on lymphocytes.ConclusionThe findings may exhibit that, although CNPs did not significantly perturb the native conformation of HHb, they can stimulate some cellular adverse effects at high concentrations that may limit the medicinal and biological application of CNPs. In other words, CNP application in biological systems should be done at low concentrations.

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“…Other approaches, like fluorescence lifetime measurements, are new methods to distinguish dynamic and static quenching mechanisms. The quenching mechanism can be further confirmed when time‐resolved fluorescence techniques are available …”

Section: Resultsmentioning

confidence: 88%

Inhibitory effect of corosolic acid on α‐glucosidase: kinetics, interaction mechanism, and molecular simulation

Pan

et al. 2019

J Sci Food Agric

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BACKGROUND The suppression of α‐glucosidase activity to retard glucose absorption is an important therapy for type‐2 diabetes. Corosolic acid (CRA) is a potential antidiabetic component in many plant‐based foods and herbs. In this study, the interplay mechanism between α‐glucosidase and corosolic acid was investigated by several methods, including three‐dimensional fluorescence spectra, circular dichroism spectra, and molecular simulation. RESULTS Corosolic acid significantly inhibited α‐glucosidase reversibly in an uncompetitive manner and its IC50 value was 1.35 × 10−5 mol L−1. A combination of CRA with myricetin exerted a weak synergy against α‐glucosidase. The intrinsic fluorescence of α‐glucosidase was quenched via a static quenching course and the binding constant was 3.47 × 103 L mol−1 at 298 K. The binding of CRA to α‐glucosidase was mainly driven by hydrophobic forces and resulted in a partial extension of the protein polypeptide chain with a loss of α‐helix content. The molecular simulation illustrated that CRA bound to the entrance part of the active center of α‐glucosidase and interacted with the amino acid residues Ser157, Arg442, Phe303, Arg315, Tyr158, and Gln353, which could hinder the release of substrate and catalytic reaction product, eventually suppressing the catalytic activity of α‐glucosidase. CONCLUSIONS These results may suggest new insights into corosolic acid from food sources as a potential α‐glucosidase inhibitor that could better control diabetes. © 2019 Society of Chemical Industry

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Hydrogen bonding-assisted interaction between amitriptyline hydrochloride and hemoglobin: spectroscopic and molecular dynamics studies

Cited by 36 publications

References 80 publications

Esterase activity and conformational changes of bovine serum albumin toward interaction with mephedrone: Spectroscopic and computational studies

Esterase activity and conformational changes of bovine serum albumin toward interaction with mephedrone: Spectroscopic and computational studies

Biophysical, docking, and cellular studies on the effects of cerium oxide nanoparticles on blood components: in vitro

Inhibitory effect of corosolic acid on α‐glucosidase: kinetics, interaction mechanism, and molecular simulation

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