24 results on '"Jitendra Kumar Maurya"'
Search Results
2. Semidefinite Multiobjective Mathematical Programming Problems with Vanishing Constraints Using Convexificators
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Kin Keung Lai, Mohd Hassan, Sanjeev Kumar Singh, Jitendra Kumar Maurya, and Shashi Kant Mishra
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multiobjective programs with vanishing constraints ,semidefinite programming ,convexificators ,nonsmooth analysis ,constraint qualifications ,Thermodynamics ,QC310.15-319 ,Mathematics ,QA1-939 ,Analysis ,QA299.6-433 - Abstract
In this paper, we establish Fritz John stationary conditions for nonsmooth, nonlinear, semidefinite, multiobjective programs with vanishing constraints in terms of convexificator and introduce generalized Cottle type and generalized Guignard type constraints qualification to achieve strong S—stationary conditions from Fritz John stationary conditions. Further, we establish strong S—stationary necessary and sufficient conditions, independently from Fritz John conditions. The optimality results for multiobjective semidefinite optimization problem in this paper is related to two recent articles by Treanta in 2021. Treanta in 2021 discussed duality theorems for special class of quasiinvex multiobjective optimization problems for interval-valued components. The study in our article can also be seen and extended for the interval-valued optimization motivated by Treanta (2021). Some examples are provided to validate our established results.
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- 2021
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3. Multiobjective Convex Optimization in Real Banach Space
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Kin Keung Lai, Mohd Hassan, Jitendra Kumar Maurya, Sanjeev Kumar Singh, and Shashi Kant Mishra
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multiobjective programming ,nonlinear programming ,convex optimization ,saddle point ,Mathematics ,QA1-939 - Abstract
In this paper, we consider convex multiobjective optimization problems with equality and inequality constraints in real Banach space. We establish saddle point necessary and sufficient Pareto optimality conditions for considered problems under some constraint qualifications. These results are motivated by the symmetric results obtained in the recent article by Cobos Sánchez et al. in 2021 on Pareto optimality for multiobjective optimization problems of continuous linear operators. The discussions in this paper are also related to second order symmetric duality for nonlinear multiobjective mixed integer programs for arbitrary cones due to Mishra and Wang in 2005. Further, we establish Karush–Kuhn–Tucker optimality conditions using saddle point optimality conditions for the differentiable cases and present some examples to illustrate our results. The study in this article can also be seen and extended as symmetric results of necessary and sufficient optimality conditions for vector equilibrium problems on Hadamard manifolds by Ruiz-Garzón et al. in 2019.
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- 2021
- Full Text
- View/download PDF
4. Multiobjective approximate gradient projection method for constrained vector optimization: Sequential optimality conditions without constraint qualifications.
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Kin Keung Lai, Jitendra Kumar Maurya, and Shashi Kant Mishra
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- 2022
- Full Text
- View/download PDF
5. Evaluation of ground water quality and health risk assessment due to nitrate and fluoride in the Middle Indo-Gangetic plains of India
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Satya Narayana Pradhan, Seema, Jitendra Kumar Maurya, and A. K. Ghosh
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Pollutant ,021110 strategic, defence & security studies ,Health risk assessment ,Health, Toxicology and Mutagenesis ,Ecological Modeling ,0211 other engineering and technologies ,02 engineering and technology ,Pollution ,Hazard quotient ,chemistry.chemical_compound ,chemistry ,Nitrate ,Environmental science ,Health risk ,Water resource management ,Fluoride ,Groundwater ,Ground water quality - Abstract
Fluoride and nitrate are the most widespread toxic pollutant elements present in groundwaters in large parts of India. The study assessed the groundwater quality and non-carcinogenic health risk du...
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- 2020
6. Ionic Liquid Green Assembly-Mediated Migration of Piperine from Calf-Thymus DNA: A New Possibility of the Tunable Drug Delivery System
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Jitendra Kumar Maurya, Rajan Patel, Neha Maurya, Zahoor Ahmad Parray, and Asimul Islam
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musculoskeletal diseases ,Circular dichroism ,General Chemical Engineering ,fungi ,General Chemistry ,C4mim ,Micelle ,Article ,Chemistry ,chemistry.chemical_compound ,chemistry ,Ionic liquid ,Drug delivery ,Biophysics ,Molecule ,lipids (amino acids, peptides, and proteins) ,Absorption (chemistry) ,QD1-999 ,Fluorescence anisotropy - Abstract
Biocompatible surface-active ionic liquid (SAIL) was used first to study the deintercalation process of a well-known natural compound piperine (PIP) as an anticancer drug, obtained from PIP–calf thymus DNA (ctDNA) complex under controlled experimental conditions. In this study, we have been exploring the interaction of PIP in SAIL (1-butyl-3-methylimidazolium octyl sulfate ionic liquid ([C4mim][C8OSO3])), ctDNA, and deintercalation of PIP from the PIP–ctDNA complex through SAIL micelle using various spectroscopic techniques. Absorption, emission, and lifetime decay measurements provide strong evidence of the relocation of PIP molecules from ctDNA to SAIL micelle. Fluorescence quenching and steady-state fluorescence anisotropy were employed to examine the exact location of PIP in different media. Moreover, the surface tension technique was also employed to confirm the release of PIP molecules from the PIP–ctDNA complex in the presence of SAIL. Circular dichroism analysis suggested that SAIL micelle does not perturb the ctDNA structure, which supported the fact that SAIL micelle can be used as a safe vehicle for PIP. Overall, the study highlighted a novel strategy for deintercalation of drug using SAIL because the release of the drug can be controlled over a period by varying the concentration and composition of the SAIL.
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- 2019
7. Multiobjective Convex Optimization in Real Banach Space
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Jitendra Kumar Maurya, Shashi Kant Mishra, Kin Keung Lai, Mohd Hassan, and Sanjeev Kumar Singh
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saddle point ,convex optimization ,Physics and Astronomy (miscellaneous) ,General Mathematics ,Pareto principle ,Banach space ,Mathematics::Optimization and Control ,Duality (optimization) ,multiobjective programming ,Nonlinear programming ,Chemistry (miscellaneous) ,Hadamard transform ,Saddle point ,Convex optimization ,Computer Science (miscellaneous) ,nonlinear programming ,QA1-939 ,Applied mathematics ,Differentiable function ,Mathematics - Abstract
In this paper, we consider convex multiobjective optimization problems with equality and inequality constraints in real Banach space. We establish saddle point necessary and sufficient Pareto optimality conditions for considered problems under some constraint qualifications. These results are motivated by the symmetric results obtained in the recent article by Cobos Sánchez et al. in 2021 on Pareto optimality for multiobjective optimization problems of continuous linear operators. The discussions in this paper are also related to second order symmetric duality for nonlinear multiobjective mixed integer programs for arbitrary cones due to Mishra and Wang in 2005. Further, we establish Karush–Kuhn–Tucker optimality conditions using saddle point optimality conditions for the differentiable cases and present some examples to illustrate our results. The study in this article can also be seen and extended as symmetric results of necessary and sufficient optimality conditions for vector equilibrium problems on Hadamard manifolds by Ruiz-Garzón et al. in 2019.
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- 2021
8. Duality in Multiobjective Mathematical Programs with Equilibrium Constraints
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Shashi Kant Mishra, Kunwar V. K. Singh, and Jitendra Kumar Maurya
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021103 operations research ,Computer science ,Applied Mathematics ,MathematicsofComputing_NUMERICALANALYSIS ,0211 other engineering and technologies ,Duality (optimization) ,02 engineering and technology ,Construct (python library) ,Type (model theory) ,Special class ,Dual (category theory) ,Nonlinear programming ,Algebra ,Computational Mathematics ,Computational Science and Engineering ,021108 energy - Abstract
In present article, we study a special class of nonlinear programming problems known as multiobjective mathematical programs with equilibrium constraints. We propose Wolfe type and Mond-Weir type dual models for multiobjective mathematical program with equilibrium constraints and establish fundamental duality results. Furthermore, we construct some examples to favor our established results.
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- 2021
9. Optimality and Duality of Pseudolinear Multiobjective Mathematical Programs with Vanishing Constraints
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Shashi Kant Mishra, Jitendra Kumar Maurya, and Avanish Shahi
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Algebra ,Optimization problem ,Dual model ,Duality (optimization) ,Type (model theory) ,Special class ,Mathematics - Abstract
In this chapter, we establish necessary and sufficient optimality conditions for a special class of optimization problems called multiobjective mathematical programs with vanishing constraints under pseudolinear assumption. We propose Mond–Weir type dual model for the considered problem and establish usual duality results. Furthermore, we present some examples to validate our results.
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- 2021
10. Interaction of promethazine and adiphenine to human hemoglobin: A comparative spectroscopic and computational analysis
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Neha Maurya, Mehraj ud din Parray, Jitendra Kumar Maurya, Amit Kumar, and Rajan Patel
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0301 basic medicine ,030103 biophysics ,Circular dichroism ,02 engineering and technology ,Molecular Dynamics Simulation ,Promethazine ,Fluorescence ,Analytical Chemistry ,Hydrophobic effect ,Hemoglobins ,03 medical and health sciences ,chemistry.chemical_compound ,Molecular dynamics ,Fluorescence Resonance Energy Transfer ,Humans ,Diphenylacetic Acids ,Instrumentation ,Spectroscopy ,Binding Sites ,Hydrogen bond ,Hydrogen Bonding ,021001 nanoscience & nanotechnology ,Atomic and Molecular Physics, and Optics ,Adiphenine ,Molecular Docking Simulation ,Spectrometry, Fluorescence ,Förster resonance energy transfer ,chemistry ,Biophysics ,Time-resolved spectroscopy ,0210 nano-technology ,Protein Binding - Abstract
The binding nature of amphiphilic drugs viz. promethazine hydrochloride (PMT) and adiphenine hydrochloride (ADP), with human hemoglobin (Hb) was unraveled by fluorescence, absorbance, time resolved fluorescence, fluorescence resonance energy transfer (FRET) and circular dichroism (CD) spectral techniques in combination with molecular docking and molecular dynamic simulation methods. The steady state fluorescence spectra indicated that both PMT and ADP quenches the fluorescence of Hb through static quenching mechanism which was further confirmed by time resolved fluorescence spectra. The UV-Vis spectroscopy suggested ground state complex formation. The activation energy (Ea) was observed more in the case of Hb-ADP than Hb-PMT interaction system. The FRET result indicates the high probability of energy transfer from β Trp37 residue of Hb to the PMT (r=2.02nm) and ADP (r=2.33nm). The thermodynamic data reveal that binding of PMT with Hb are exothermic in nature involving hydrogen bonding and van der Waal interaction whereas in the case of ADP hydrophobic forces play the major role and binding process is endothermic in nature. The CD results show that both PMT and ADP, induced secondary structural changes of Hb and unfold the protein by losing a large helical content while the effect is more pronounced with ADP. Additionally, we also utilized computational approaches for deep insight into the binding of these drugs with Hb and the results are well matched with our experimental results.
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- 2018
11. Effect of aromatic amino acids on the surface properties of 1-dodecyl-3-(4-(3-dodecylimidazolidin-1-yl)butyl)imidazolidine bromide gemini surfactant
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Anwar Ali, Abbul Bashar Khan, Amit Kumar, Rajan Patel, Jitendra Kumar Maurya, and Neeraj Dohare
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chemistry.chemical_classification ,Polymers and Plastics ,Thermodynamics of micellization ,02 engineering and technology ,010402 general chemistry ,021001 nanoscience & nanotechnology ,01 natural sciences ,0104 chemical sciences ,Surfaces, Coatings and Films ,Amino acid ,Hydrophobic effect ,chemistry.chemical_compound ,chemistry ,Pulmonary surfactant ,Imidazolidine ,Bromide ,Ionic liquid ,Polymer chemistry ,Aromatic amino acids ,Organic chemistry ,lipids (amino acids, peptides, and proteins) ,Physical and Theoretical Chemistry ,0210 nano-technology - Abstract
Herein, we have studied the micellization of imidazolium-based ionic liquid type gemini surfactant ([C12-4-C12im]Br2) in the absence and presence of aromatic amino acids by conductivity and surface...
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- 2017
12. In Vitro Cytotoxicity and Interaction of Noscapine with Human Serum Albumin: Effect on Structure and Esterase Activity of HSA
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Neha Maurya, Upendra Kumar Singh, Meena Kumari, Zafaryab, Rajan Patel, Ravins Dohare, Meher Rizvi, and Jitendra Kumar Maurya
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Noscapine ,Circular dichroism ,Skin Neoplasms ,Population ,Static Electricity ,Pharmaceutical Science ,Serum Albumin, Human ,02 engineering and technology ,In Vitro Techniques ,Molecular Dynamics Simulation ,030226 pharmacology & pharmacy ,Fluorescence spectroscopy ,Protein Structure, Secondary ,03 medical and health sciences ,0302 clinical medicine ,Cell Line, Tumor ,Drug Discovery ,Spectroscopy, Fourier Transform Infrared ,medicine ,Fluorescence Resonance Energy Transfer ,Humans ,Protein Interaction Domains and Motifs ,education ,education.field_of_study ,Quenching (fluorescence) ,Binding Sites ,Cell Death ,Chemistry ,Circular Dichroism ,Esterases ,021001 nanoscience & nanotechnology ,Human serum albumin ,Fluorescence ,Molecular Docking Simulation ,Förster resonance energy transfer ,Biophysics ,Molecular Medicine ,Thermodynamics ,0210 nano-technology ,Hydrophobic and Hydrophilic Interactions ,medicine.drug ,Protein Binding - Abstract
Noscapine is effective to inhibit cellular proliferation and induced apoptosis in nonsmall cell, lung, breast, lymphoma, and prostate cancer. It also shows good efficiency to skin cancer cells. In the current work, we studied the mechanism of interaction between the anticancer drug noscapine (NOS) and carrier protein human serum albumin (HSA) by using a variety of spectroscopic techniques (fluorescence spectroscopy, time-resolved fluorescence, UV-visible, fluorescence resonance energy transfer (FRET), Fourier transform infrared (FTIR), and circular dichroism (CD) spectroscopy), electrochemistry (cyclic voltammetry), and computational methods (molecular docking and molecular dynamic simulation). The steady-state fluorescence results showed that fluorescence intensity of HSA decreased in the presence of NOS via a static quenching mechanism, which involves ground state complex formation between NOS and HSA. UV-visible and FRET results also supported the fluorescence result. The corresponding thermodynamic result shows that binding of NOS with HSA is exothermic in nature, involving electrostatic interactions as major binding forces. The binding results were further confirmed through a cyclic voltammetry approach. The FRET result signifies the energy transfer from Trp214 of HSA to the NOS. Molecular site marker, molecular docking, and MD simulation results indicated that the principal binding site of HSA for NOS is site I. Synchronous fluorescence spectra, FTIR, 3D fluorescence, CD spectra, and MD simulation results reveal that NOS induced the structural change in HSA. In addition, the MTT assay study on a human skin cancer cell line (A-431) was also performed for NOS, which shows that NOS induced 80% cell death of the population at a 320 μM concentration. Moreover, the esterase-like activity of HSA with NOS was also done to determine the variation in protein functionality after binding with NOS.
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- 2019
13. A spectroscopic and molecular dynamic approach on the interaction between ionic liquid type gemini surfactant and human serum albumin
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Jitendra Kumar Maurya, Muzaffar Ul Hassan Mir, Anwar Ali, Neha Maurya, Neeraj Dohare, and Rajan Patel
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0301 basic medicine ,030103 biophysics ,Circular dichroism ,Enthalpy ,Molecular Conformation ,Ionic Liquids ,Ionic bonding ,Nanotechnology ,Molecular Dynamics Simulation ,010402 general chemistry ,01 natural sciences ,Molecular Docking Simulation ,Hydrophobic effect ,Surface-Active Agents ,03 medical and health sciences ,symbols.namesake ,Molecular dynamics ,chemistry.chemical_compound ,Calcitriol ,Structural Biology ,Humans ,Molecular Biology ,Serum Albumin ,Binding Sites ,Spectrum Analysis ,General Medicine ,0104 chemical sciences ,Gibbs free energy ,chemistry ,Ionic liquid ,symbols ,Thermodynamics ,Physical chemistry ,Protein Binding - Abstract
The interactions of imidazolium bashed ionic liquid-type cationic gemini surfactant ([C12-4-C12im]Br2) with HSA were studied by fluorescence, time-resolved fluorescence, UV-visible, circular dichroism, molecular docking and molecular dynamic simulation methods. The results showed that the [C12-4-C12im]Br2 quenched the fluorescence of HSA through dynamic quenching mechanism as confirmed by time-resolved spectroscopy. The Stern-Volmer quenching constant (Ksv) and relevant thermodynamic parameters such as enthalpy change (ΔH), Gibbs free energy change (ΔG) and entropy change (ΔS) for interaction system were calculated at different temperatures. The results revealed that hydrophobic forces played a major role in the interactions process. The results of synchronous fluorescence, UV-visible and CD spectra demonstrated that the binding of [C12-4-C12im]Br2 with HSA induces conformational changes in HSA. Inquisitively, the molecular dynamics study contribute towards understanding the effect of binding of [C12-4-C12im]Br2 on HSA to interpret the conformational change in HSA upon binding in aqueous solution. Moreover, the molecular modelling results show the possible binding sites in the interaction system.
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- 2016
14. Molecular investigation of the interaction between ionic liquid type gemini surfactant and lysozyme: A spectroscopic and computational approach
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Rajan Patel, Jitendra Kumar Maurya, Upendra Kumar Singh, Neeraj Dohare, Neha Maurya, Seema Patel, Anwar Ali, and Muzaffar Ul Hassan Mir
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Hydrogen bond ,Organic Chemistry ,Biophysics ,Analytical chemistry ,General Medicine ,Biochemistry ,Binding constant ,Biomaterials ,Hydrophobic effect ,chemistry.chemical_compound ,Molecular dynamics ,chemistry ,Docking (molecular) ,Ionic liquid ,Physical chemistry ,Time-resolved spectroscopy ,Spectroscopy - Abstract
Herein, we are reporting the interaction of ionic liquid type gemini surfactant, 1,4-bis(3-dodecylimidazolium-1-yl) butane bromide ([C12−4-C12im]Br2) with lysozyme by using Steady state fluorescence, UV-visible, Time resolved fluorescence, Fourier transform-infrared (FT-IR) spectroscopy techniques in combination with molecular modeling and docking method. The steady state fluorescence spectra suggested that the fluorescence of lysozyme was quenched by [C12−4-C12im]Br2 through static quenching mechanism as confirmed by time resolved fluorescence spectroscopy. The binding constant for lysozyme-[C12−4-C12im]Br2 interaction have been measured by UV-visible spectroscopy and found to be 2.541 × 105M−1. The FT-IR results show conformational changes in the secondary structure of lysozyme by the addition of [C12−4-C12im]Br2. Moreover, the molecular docking study suggested that hydrogen bonding and hydrophobic interactions play a key role in the protein-surfactant binding. Additionally, the molecular dynamic simulation results revealed that the lysozyme-[C12−4-C12im]Br2 complex reaches an equilibrium state at around 3 ns. © 2015 Wiley Periodicals, Inc. Biopolymers 103: 406–415, 2015.
- Published
- 2015
15. Spectroscopic and molecular modelling analysis of the interaction between ethane-1,2-diyl bis(N,N-dimethyl-N-hexadecylammoniumacetoxy)dichloride and bovine serum albumin
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Rajan Patel, Jitendra Kumar Maurya, Mehraj ud din Parray, Anwar Ali, Upendra Kumar Singh, Neha Maurya, Abbul Bashar Khan, and Muzaffar Ul Hassan Mir
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biology ,Chemistry ,Biophysics ,Analytical chemistry ,Fluorescence ,Binding constant ,Fluorescence spectroscopy ,Hydrophobic effect ,Crystallography ,Chemistry (miscellaneous) ,Docking (molecular) ,biology.protein ,Hypsochromic shift ,Bovine serum albumin ,Spectroscopy - Abstract
Several spectroscopic approaches namely fluorescence, time-resolved fluorescence, UV-visible, and Fourier transform infra-red (FT-IR) spectroscopy were employed to examine the interaction between ethane-1,2-diyl bis(N,N-dimethyl-N-hexadecylammoniumacetoxy)dichloride (16-E2-16) and bovine serum albumin (BSA). Fluorescence studies revealed that 16-E2-16 quenched the BSA fluorescence through a static quenching mechanism, which was further confirmed by UV–visible and time-resolved fluorescence spectroscopy. In addition, the binding constant and the number of binding sites were also calculated. The thermodynamic parameters at different temperatures (298 K, 303 K, 308 K and 313 K) indicated that 16-E2-16 binding to BSA is entropy driven and that the major driving forces are electrostatic interactions. Decrease of the α-helix from 53.90 to 46.20% with an increase in random structure from 22.56 to 30.61% were also observed by FT-IR. Furthermore, the molecular docking results revealed that 16-E2-16 binds predominantly by electrostatic and hydrophobic forces to some residues in the BSA sub-domains IIA and IIIA. Copyright © 2015 John Wiley & Sons, Ltd.
- Published
- 2015
16. An insight into the binding between ester-functionalized cationic Gemini surfactant and lysozyme
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Muzaffar Ul Hassan Mir, Meena Kumari, Neha Maurya, Rajan Patel, and Jitendra Kumar Maurya
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Circular dichroism ,Enthalpy ,Biophysics ,Cationic polymerization ,General Chemistry ,Condensed Matter Physics ,Biochemistry ,Fluorescence ,Atomic and Molecular Physics, and Optics ,Gibbs free energy ,Hydrophobic effect ,chemistry.chemical_compound ,Crystallography ,symbols.namesake ,chemistry ,symbols ,Lysozyme ,Time-resolved spectroscopy - Abstract
The interactions of cationic dodecyl betainate gemini (DBG) surfactant with lysozyme was studied by fluorescence, time resolved fluorescence, UV–visible, circular dichroism, and molecular docking methods. The results showed that the DBG quenched the fluorescence of lysozyme through static quenching mechanism as confirmed by time resolved spectroscopy. The Stern–Volmer quenching constant ( K sv ) and relevant thermodynamic parameters such as enthalpy change (ΔH), Gibbs free energy change (ΔG) and entropy change (ΔS) for interaction system were calculated at different temperatures. The results revealed that hydrophobic forces played a major role in the interactions process. The results of synchronous fluorescence, UV–visible and CD spectra demonstrated that the binding of DBG with lysozyme induces conformational changes in lysozyme. Moreover, the molecular modeling results shows the possible binding sites in the interaction system.
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- 2014
17. Enthalpy-driven interaction between dihydropyrimidine compound and bovine serum albumin: a spectroscopic and computational approach
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Jitendra Kumar Maurya, Neeraj Dohare, Mehraj ud din Parray, Neha Maurya, Rajan Patel, Amit Kumar, and Manasa Kongot
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Models, Molecular ,Dihydropyridines ,Binding Sites ,biology ,010405 organic chemistry ,Chemistry ,Spectrum Analysis ,Enthalpy ,Serum Albumin, Bovine ,General Medicine ,010402 general chemistry ,01 natural sciences ,Combinatorial chemistry ,0104 chemical sciences ,Structural Biology ,biology.protein ,Animals ,Cattle ,Bovine serum albumin ,Molecular Biology ,Protein Binding - Abstract
Diazines represent an important class of heterocyclic compounds, which are known to exhibit a wide spectrum of biological activities, and the majority of these versatile compounds are the backbone ...
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- 2017
- Full Text
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18. Probing HSA-ionic liquid interactions by spectroscopic and molecular docking methods
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Jitendra Kumar Maurya, Munazzah Tasleem, Prashant Singh, Meena Kumari, and Rajan Patel
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Conformational change ,Biophysics ,Analytical chemistry ,Ionic Liquids ,Hydrophobic effect ,chemistry.chemical_compound ,symbols.namesake ,Spectroscopy, Fourier Transform Infrared ,medicine ,Humans ,Radiology, Nuclear Medicine and imaging ,Serum Albumin ,Binding Sites ,Radiation ,Radiological and Ultrasound Technology ,Hydrogen bond ,Hydrogen Bonding ,Human serum albumin ,Protein Structure, Tertiary ,Gibbs free energy ,Molecular Docking Simulation ,body regions ,Crystallography ,Spectrometry, Fluorescence ,chemistry ,Critical micelle concentration ,embryonic structures ,Ionic liquid ,Proton NMR ,symbols ,Thermodynamics ,Spectrophotometry, Ultraviolet ,Hydrophobic and Hydrophilic Interactions ,Protein Binding ,medicine.drug - Abstract
Herein, we report the interaction of synthesized pyrrolidinium based ionic liquid, N-butyl-N-methyl-2-oxopyrrolidinium bromide (BMOP) with human serum albumin (HSA). The BMOP was characterized by using (1)H NMR, (13)C NMR and FT-IR techniques. The critical micelle concentration (cmc) of BMOP was confirmed by surface tension, conductivity and contact angle measurements. The interactions between HSA and BMOP were studied by steady-state and time-resolved fluorescence, UV-visible, FT-IR spectroscopic and molecular docking methods. The steady-state fluorescence spectra showed that BMOP quenched the fluorescence of HSA through combined quenching mechanism. Corresponding thermodynamic parameters viz. Gibbs free energy change (ΔG), entropy change (ΔS) and enthalpy change (ΔH) illustrated that the binding process was spontaneous and entropy driven. It is also suggested that hydrophobic forces play a key role in the binding of BMOP to HSA. In addition, the pyrene probe analysis again suggests the involvement of hydrophobic interaction in HSA-BMOP complex formation. Surface tension profile showed that the cmc value of BMOP in the presence of HSA is higher than the cmc value of pure BMOP. The FT-IR results show a conformational change in the secondary structure of HSA upon the addition of BMOP. The molecular docking result indicated that BMOP binds with HSA at hydrophobic pocket domain IIA with hydrophobic and hydrogen bond interactions in which hydrophobic interactions are dominating.
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- 2014
19. Spectroscopic and docking studies on the interaction between pyrrolidinium based ionic liquid and bovine serum albumin
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Prashant Singh, Maroof Ali, Jitendra Kumar Maurya, Meena Kumari, Upendra Kumar Singh, Rajan Patel, and Abbul Bashar Khan
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Pyrrolidines ,Time Factors ,Enthalpy ,Analytical chemistry ,Ionic Liquids ,Molecular Dynamics Simulation ,Analytical Chemistry ,Hydrophobic effect ,chemistry.chemical_compound ,symbols.namesake ,Spectroscopy, Fourier Transform Infrared ,Animals ,Bovine serum albumin ,Instrumentation ,Protein secondary structure ,Spectroscopy ,Binding Sites ,Quenching (fluorescence) ,biology ,Hydrogen bond ,Chemistry ,Temperature ,Serum Albumin, Bovine ,Atomic and Molecular Physics, and Optics ,Gibbs free energy ,Molecular Docking Simulation ,Kinetics ,Crystallography ,Spectrometry, Fluorescence ,Ionic liquid ,biology.protein ,symbols ,Cattle ,Spectrophotometry, Ultraviolet - Abstract
The interaction of synthesized ionic liquid, 1-butyl-1-methyl-2-oxopyrrolidinium bromide (BMOP) and bovine serum albumin (BSA) was investigated using UV-Vis, FT-IR, steady state and time resolved fluorescence measurements and docking studies. Steady state spectra revealed that BMOP strongly quenched the intrinsic fluorescence of BSA through dynamic quenching mechanism. The corresponding thermodynamic parameters; Gibbs free energy change (ΔG), entropy change (ΔS) and enthalpy change (ΔH) showed that the binding process was spontaneous and entropy driven. It is also indicated that hydrophobic forces play a key role in the binding of BMOP to BSA. The synchronous fluorescence spectroscopy reveals that the conformation of BSA changed in the presence of BMOP. The shift in amide I band of FT-IR spectrum of BSA suggested unfolding of the protein secondary structure upon the addition of BMOP. In addition, the molecular modeling study of BSA-BMOP system shows that BMOP binds with BSA at the interface between two sub domains IIA and IIIA, which is located just above the entrance of the binding pocket of IIA through hydrophobic and hydrogen bond interactions in which hydrophobic interaction are dominated.
- Published
- 2014
20. Molecular interaction of cationic gemini surfactant with bovine serum albumin: A spectroscopic and molecular docking study
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Jitendra Kumar Maurya, Shah Ubaid-ullah, Muzaffar Ul Hassan Mir, Abbul Bashar Khan, Rajan Patel, and Shahnawaz Ali
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Circular dichroism ,Quenching (fluorescence) ,Hydrodynamic radius ,biology ,Hydrogen bond ,Chemistry ,Analytical chemistry ,Bioengineering ,Applied Microbiology and Biotechnology ,Biochemistry ,Fluorescence ,Hydrophobic effect ,Crystallography ,Dynamic light scattering ,biology.protein ,Bovine serum albumin - Abstract
Herein, we report the effect of N,N′-bis(dodecyloxycarbonylmethyl)-N,N,N′,N′-tetramethyl-1,2-ethanediammonium dibromide (dodecyl betainate gemini or DBG) on the structure and function of bovine serum albumin (BSA) by using fluorescence, time resolved fluorescence, circular dichroism and dynamic light scattering techniques. The Stern–Volmer quenching constants KSV and the corresponding thermodynamic parameters viz ΔH, ΔG and ΔS have been estimated by the fluorescence quenching method. The results indicated that DBG binds spontaneously with BSA through hydrophobic interaction. Time resolved fluorescence data show that the quenching follows the static mechanism pathway. It can be seen from far-UV CD spectra that the α-helical network of BSA is disrupted and its content increases from 71% to 79% at lower concentrations which again decreases to 38% at higher concentration. DLS measurements suggested that hydrodynamic radius (Rh) decreases in the presence of 30 and 40 μM of DBG while it increases when the concentration of DBG was 70 and 100 μM. The molecular docking study indicated that DBG is embedded into subdomain IIA of BSA and binds with the R-914, R-195 and R-217 residues by hydrogen bonding and by hydrophobic interaction.
- Published
- 2014
21. Stable graphite exfoliation by fullerenol intercalation via aqueous route
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Jitendra Kumar Maurya, Suresh Chand, Jitendra Gaur, Rachana Kumar, Niharika Saxena, Pramod Kumar, Samya Naqvi, and Neha Gupta
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Fullerene ,Graphene ,Intercalation (chemistry) ,Nanotechnology ,Graphite oxide ,General Chemistry ,Exfoliation joint ,Catalysis ,law.invention ,chemistry.chemical_compound ,symbols.namesake ,Chemical engineering ,chemistry ,law ,Materials Chemistry ,symbols ,Graphite ,Raman spectroscopy ,Graphene oxide paper - Abstract
Graphene is a wonder material possessing unique properties; however, graphene prepared by exfoliation of graphite has property to restack because of van der Waals interactions to form graphite. This restacking can be prevented by insertion of large molecules like fullerene, which not only exfoliates graphite layer but also prevents restacking of prepared graphene sheets. The present article also describes a mild method of graphite oxide synthesis (GO) for lower degree of oxidation resulting in less defected (ruptured carbon framework) graphene sheets. Exfoliation is performed by intercalation of large fullerene molecules by aqueous reaction of fullerene hydroxide (fullerenol) with the epoxy functionalities on graphite oxide to prepare fullerene intercalated graphite (G-Fol). Fullerene functionalization of GO to form G-Fol has been established by FTIR spectroscopy, UV-Vis spectroscopy, TGA and number of layers has been ascertained by Raman spectroscopy, XRD and HRTEM. Stable exfoliation of G-Fol has been confirmed by change in absorbance with time. Photoluminescence property of the material is also evaluated by fluorescence emission and excitation measurement at different excitation and emission wavelengths, respectively. The present article explains a new method of exfoliation of graphite to form stable functionalized graphene layers with fewer defects for future applications as buffer layer in electronic devices.
- Published
- 2014
22. Hydrogen bonding-assisted interaction between amitriptyline hydrochloride and hemoglobin: spectroscopic and molecular dynamics studies
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Rajan Patel, Meena Kumari, Abbul Bashar Khan, Ravins Dohare, Jitendra Kumar Maurya, and Neha Maurya
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0301 basic medicine ,030103 biophysics ,Circular dichroism ,Stereochemistry ,Amitriptyline ,Molecular Conformation ,Molecular Dynamics Simulation ,010402 general chemistry ,01 natural sciences ,Molecular Docking Simulation ,Fluorescence spectroscopy ,03 medical and health sciences ,Molecular dynamics ,Hemoglobins ,Structural Biology ,Humans ,Spectroscopy ,Molecular Biology ,Quenching (fluorescence) ,Binding Sites ,Chemistry ,Hydrogen bond ,Spectrum Analysis ,Hydrogen Bonding ,General Medicine ,Binding constant ,0104 chemical sciences ,Crystallography ,Thermodynamics ,Protein Binding - Abstract
Herein, we have explored the interaction between amitriptyline hydrochloride (AMT) and hemoglobin (Hb), using steady-state and time-resolved fluorescence spectroscopy, UV-visible spectroscopy, and circular dichroism spectroscopy, in combination with molecular docking and molecular dynamic (MD) simulation methods. The steady-state fluorescence reveals the static quenching mechanism in the interaction system, which was further confirmed by UV-visible and time-resolved fluorescence spectroscopy. The binding constant, number of binding sites, and thermodynamic parameters viz. ΔG, ΔH, ΔS are also considered; result confirms that the binding of the AMT with Hb is a spontaneous process, involving hydrogen bonding and van der Waals interactions with a single binding site, as also confirmed by molecular docking study. Synchronous fluorescence, CD data, and MD simulation results contribute toward understanding the effect of AMT on Hb to interpret the conformational change in Hb upon binding in aqueous solution.
- Published
- 2016
23. Molecular investigation of the interaction between ionic liquid type gemini surfactant and lysozyme: A spectroscopic and computational approach
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Jitendra Kumar, Maurya, Muzaffar Ul Hassan, Mir, Upendra Kumar, Singh, Neha, Maurya, Neeraj, Dohare, Seema, Patel, Anwar, Ali, and Rajan, Patel
- Subjects
Surface-Active Agents ,Spectrometry, Fluorescence ,Circular Dichroism ,Spectroscopy, Fourier Transform Infrared ,Ionic Liquids ,Hydrogen Bonding ,Muramidase ,Hydrophobic and Hydrophilic Interactions ,Protein Binding - Abstract
Herein, we are reporting the interaction of ionic liquid type gemini surfactant, 1,4-bis(3-dodecylimidazolium-1-yl) butane bromide ([C12-4-C12 im]Br2) with lysozyme by using Steady state fluorescence, UV-visible, Time resolved fluorescence, Fourier transform-infrared (FT-IR) spectroscopy techniques in combination with molecular modeling and docking method. The steady state fluorescence spectra suggested that the fluorescence of lysozyme was quenched by [C12-4-C12 im]Br2 through static quenching mechanism as confirmed by time resolved fluorescence spectroscopy. The binding constant for lysozyme-[C12-4-C12 im]Br2 interaction have been measured by UV-visible spectroscopy and found to be 2.541 × 10(5) M(-1). The FT-IR results show conformational changes in the secondary structure of lysozyme by the addition of [C12-4-C12 im]Br2. Moreover, the molecular docking study suggested that hydrogen bonding and hydrophobic interactions play a key role in the protein-surfactant binding. Additionally, the molecular dynamic simulation results revealed that the lysozyme-[C12-4-C12 im]Br2 complex reaches an equilibrium state at around 3 ns.
- Published
- 2014
24. Spectroscopic and molecular modelling analysis of the interaction between ethane-1,2-diyl bis(N,N-dimethyl-N-hexadecylammoniumacetoxy)dichloride and bovine serum albumin
- Author
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Rajan, Patel, Muzaffar Ul Hassan, Mir, Jitendra Kumar, Maurya, Upendra Kumar, Singh, Neha, Maurya, Mehraj, ud din Parray, Abbul Bashar, Khan, and Anwar, Ali
- Subjects
Models, Molecular ,Molecular Docking Simulation ,Quaternary Ammonium Compounds ,Kinetics ,Spectroscopy, Fourier Transform Infrared ,Glycine ,Animals ,Cattle ,Serum Albumin, Bovine ,Spectrophotometry, Ultraviolet ,Fluorescence ,Protein Binding - Abstract
Several spectroscopic approaches namely fluorescence, time-resolved fluorescence, UV-visible, and Fourier transform infra-red (FT-IR) spectroscopy were employed to examine the interaction between ethane-1,2-diyl bis(N,N-dimethyl-N-hexadecylammoniumacetoxy)dichloride (16-E2-16) and bovine serum albumin (BSA). Fluorescence studies revealed that 16-E2-16 quenched the BSA fluorescence through a static quenching mechanism, which was further confirmed by UV-visible and time-resolved fluorescence spectroscopy. In addition, the binding constant and the number of binding sites were also calculated. The thermodynamic parameters at different temperatures (298 K, 303 K, 308 K and 313 K) indicated that 16-E2-16 binding to BSA is entropy driven and that the major driving forces are electrostatic interactions. Decrease of the α-helix from 53.90 to 46.20% with an increase in random structure from 22.56 to 30.61% were also observed by FT-IR. Furthermore, the molecular docking results revealed that 16-E2-16 binds predominantly by electrostatic and hydrophobic forces to some residues in the BSA sub-domains IIA and IIIA.
- Published
- 2014
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