Eva Judy

@iitb.ac.in

IIT Bombay



           

https://researchid.co/evajudy
2

Scopus Publications

35

Scholar Citations

1

Scholar h-index

1

Scholar i10-index

Scopus Publications

  • Analytical Aspects of ANSA-BSA Association: A Thermodynamic and Conformational Approach
    Anu Jain, Eva Judy, and Nand Kishore
    American Chemical Society (ACS)
    Many studies have demonstrated the manner in which ANS interacts with bovine serum albumin (BSA), although they are limited by the extremely low solubility of dye. The present study demonstrates the binding of ANSA dye with BSA, and since this dye can easily replace ANS, it not only simplifies research but also improves sensor accuracy for serum albumin. A combination of calorimetry and spectroscopy has been employed to establish the thermodynamic signatures associated with the interaction of ANSA with the protein and the consequent conformational changes in the latter. The results of differential scanning calorimetry reveal that when the concentration of ANSA in solution is increased, the thermal stability of the protein increases substantially. The fluorescence data demonstrated a decrease in the binding affinity of ANSA with the protein when pH increased but was unable to identify a change in the mode of interaction of the ligand. ITC has demonstrated that the mode of interaction between ANSA and the protein varies from a single set of binding sites at pH 5 and 7.4 to a sequential binding site at pH 10, emphasizing the potential relevance of protein conformational changes. TCSPC experiments suggested a dynamic type in the presence of ANSA. Molecular docking studies suggest that ANSA molecules are able to find ionic centers in the hydrophobic pockets of BSA. The findings further imply that given its ease of use in experiments, ANSA may be a useful probe for tracking the presence of serum albumin and partially folded protein states.



  • Mechanistic insights into encapsulation and release of drugs in colloidal niosomal systems: Biophysical aspects
    Eva Judy, Manu Lopus, and Nand Kishore
    Royal Society of Chemistry (RSC)
    Vesicular systems such as niosomes provide an alternative to improve drug delivery systems.

  • Correlating the Properties of Antibiotics with the Energetics of Partitioning in Colloidal Self-Assemblies and the Effect on the Binding of a Released Drug with a Target Protein
    Eva Judy and Nand Kishore
    American Chemical Society (ACS)
    The bioavailability of drugs and the monitoring of efficient dosage requires drug delivery through suitable vehicles. The partitioning characteristics of the drugs in the delivery vehicles is determined by their molecular features and structure. A quantitative understanding of the partitioning of drugs into delivery media and its subsequent release and binding to the target protein is essential to deriving guidelines for rational drug design. We have studied the partitioning of aminoglycosides and macrolide antibiotic drugs kanamycin, gentamicin, azithromycin, and erythromycin in cationic, nonionic, and the mixture of cationic and nonionic self-assemblies. The quantitative aspects of drug partitioning followed by the monitoring of its interaction with target model protein bovine serum albumin on subsequent release have been performed by using a combination of spectroscopy and high-sensitivity calorimetry. The mechanisms of partitioning have been analyzed on the basis of the values of standard molar enthalpy, entropy, the Gibbs free-energy change, and stoichiometry of interaction. The integrity of the binding sites and the effects of the components of the self-assemblies and the released drug on the serum albumin were analyzed by using differential scanning calorimetry and circular dichroism spectroscopy. The thermodynamic signatures of drug partitioning and subsequent binding to target protein have enabled an in-depth correlation of the structure-property-energetics relationships which are crucial for the broader objective of rational drug design.

  • Quantitative calorimetric evidences into counteraction mechanism of denaturing effect of guanidine hydrochloride by citrulline and betaine
    Eva Judy and Nand Kishore
    Elsevier BV
    Abstract Obtaining qualitative and quantitative insights into counteraction mechanism of deleterious effects of denaturants on proteins is crucial because of its fundamental impact on biological and industrial processes. In this work, we have employed a combination of ultrasensitive isothermal titration calorimetry and differential scanning calorimetry in understanding the mechanistic aspects of scarcely studied counteraction of denaturing action of guanidine hydrochloride by citrulline, betaine and their combination. The results have enabled a quantitative evaluation of stabilization provided by these biologically important molecules along with insights into the counteraction mechanism on the basis of energetics and strength of interactions. Citrulline is able to provide better stabilization to the protein under stressed environment of guanidine hydrochloride than betaine which stabilizes by a relatively different mechanism. The results suggest that along with weak polar interactions between these molecules and guanidine hydrochloride which tend to pull back the denaturant from the protein surface, preferential exclusion also plays a major role. This conclusion differs from the suggested mode of counteraction of urea by osmolytes based mostly on theoretical considerations which emphasize on engagement of osmolytes with urea, though experimental evidences are still lacking for the same.

  • Discrepancies in thermodynamic information obtained from calorimetry and spectroscopy in ligand binding reactions: Implications on correct analysis in systems of biological importance
    Eva Judy and Nand Kishore
    The Chemical Society of Japan
    Thermodynamic signatures accompanying ligand binding interactions with proteins and nucleic acids have great potential in drug discovery and help in deriving guidelines for rational drug design. Fr...

  • Partitioning of anticancer drug 5-fluorouracil in micellar media explored by physicochemical properties and energetics of interactions: Quantitative insights for implications in drug delivery
    Moumita Dasgupta, Eva Judy, and Nand Kishore
    Elsevier BV
    Drug delivery vehicles such as micelles, vesicles and other nanoemulsions are necessary for enhanced bioavailability of drugs in the body. We have measured and correlated physicochemical properties of an anticancer drug 5-fluorouracil in the micelles of anionic surfactant sodium dodecyl sulfate. cationic surfactant hexadecyltrimethylammonium bromide, and non-ionic surfactant triton X-100 with the energetics of interactions. Thermodynamic signatures accompanying the partitioning of drug into surfactant micelles along with standard partial molar volume and standard partial molar compressibilities of transfer from water to the micelles have been interpreted in terms of strength, nature and extent of partitioning. Functional groups on the drug responsible for interaction/partitioning in micelles have been identified. Interaction of 5-fluorouracil in two or three sequential partitioning behavior depending on the nature of the surfactant micelles has enabled detailed mechanistic analysis of the partitioning process. Structure-property-energetics relationship to obtain deeper insights into the nature of interaction between the drug and micelles has been addressed. Such studies provide information on the significance of functional groups on the drug molecule which can be modified for optimum partitioning in drug delivery vehicles to account for effective target oriented release.

  • A look back at the molten globule state of proteins: thermodynamic aspects
    Eva Judy and Nand Kishore
    Springer Science and Business Media LLC
    Interest in protein folding intermediates lies in their significance to protein folding pathways. The molten globule (MG) state is one such intermediate lying on the kinetic (and sometimes thermodynamic) pathway between native and unfolded states. Development of our qualitative and quantitative understanding of the MG state can provide deeper insight into the folding pathways and hence potentially facilitate solution of the protein folding problem. An extensive look at literature suggests that most studies into protein MG states have been largely qualitative. Attempts to obtain quantitative insights into MG states have involved application of high-sensitivity calorimetry (differential scanning calorimetry and isothermal titration calorimetry). This review addresses the progress made in this direction by discussing the knowledge gained to date, along with the future promise of calorimetry, in providing quantitative information on the structural features of MG states. Particular attention is paid to the question of whether such states share common structural features or not. The difference in the nature of the transition from the MG state to the unfolded state, in terms of cooperativity, has also been addressed and discussed.

  • 1,1,1,3,3,3-Hexafluoroisopropanol and 2,2,2-trifluoroethanol act more effectively on protein in combination than individually: Thermodynamic aspects
    Niki S. Jha, Eva Judy, and Nand Kishore
    Elsevier BV
    Abstract 2,2,2-Trifluoroethanol (TFE) and 1,1,1,3,3,3-hexafluoroisopropanol (HFIP) are known to be secondary structure inducers of proteins. In order to determine the efficacy of TFE and HFIP in affecting the conformation of proteins when taken together, as compared to individually, we have studied the thermodynamics of unfolding of bovine serum albumin (BSA) in the presence of these alcohols along with the conformational characterization of the protein. A comparison of change in thermal transition temperature of the protein in the absence and presence of these alcohols in combination and individually shows that the (TFE+HFIP) mixture is a stronger stabilizer of BSA up to a certain molality as compared to addition of their individual effects. The thermodynamics of effects of these alcohols on dithiotheitol reduced BSA were also studied. The enthalpies of interaction of TFE with HFIP in aqueous solution were measured by using isothermal titration calorimetry. The endothermic molar enthalpy of interaction of TFE with HFIP suggests that these alcohols do not strongly associate with each other through polar interactions. This is a possible explanation for their stronger effect on protein stability and conformation in combination rather than individually. The circular dichroism and fluorescence spectroscopic results provide evidence for the enhancement of the secondary structure of the protein by TFE and HFIP along with internalization of tryptophan residues in more hydrophobic environment.

  • Physicochemical properties of L-carnitine in aqueous solution and its interaction with trimethylamine N-oxide, sodium chloride and dextrose: Volumetric and calorimetric insights
    Anju Arya, Eva Judy, and Nand Kishore
    Elsevier BV
    Abstract L -carnitine plays physiologically important roles specifically to decrease triglycerides, very low density lipoprotein (VLDL) and cholesterol. Considering these facts, it is believed to be helpful in the reduction of cardiovascular diseases and diabetes. Physicochemical properties of L -carnitine in aqueous or mixed aqueous solutions are scarcely available in literature. Such properties will be useful in understanding the interactions of L -carnitine with other cellular components like trimethylamine-N-oxide (TMAO), dextrose ( D -glucose) and NaCl. The values of densities (ρ) and speeds of sound (u) of L -carnitine were measured over the molality range of m = 0.05 mol·kg−1 to m = 0.3 mol·kg−1 at temperature T = 293.15 K to T = 313.15 K in water and in aqueous solutions of TMAO, dextrose, and NaCl. Using these data, values of apparent molar volume (V2,m,φ) and apparent molar adiabatic compressibility (Ks,2,m,φ) have been determined. The results obtained from these measurements have been used to derive the standard partial molar volume ( V 2 , m o ), standard partial molar adiabatic compressibility ( K s , 2 , m o ), standard partial molar volume of transfer ( Δ tr V 2 , m o ) and standard partial molar isentropic compressibilities of transfer ( Δ tr K S , 2 , m o ) from water to aqueous solutions of TMAO, dextrose, and NaCl. Through Isothermal Titration Calorimetry (ITC), the enthalpies of dilution ( Δ dil H m ) of L -carnitine in water (over a temperature range of T = 293.15 K to T = 313.15 K) and in aqueous solutions of TMAO, dextrose, and NaCl have been determined. The values of standard molar enthalpy of dilution ( Δ dil H m o ) and their transfer values ( Δ tr Δ dil H m o ) have been derived from these measurements. The results have been discussed in terms of possible intermolecular interactions. The data suggest that there is overall balancing of hydrophobic and hydrophilic interactions in system containing L -carnitine and TMAO in aqueous solution, but hydrophobic effect dominates when the co-solute is NaCl or dextrose.

  • Drug Partitioning in Micellar Media and Its Implications in Rational Drug Design: Insights with Streptomycin
    Eva Judy, Darshna Pagariya, and Nand Kishore
    American Chemical Society (ACS)
    Oral bioavailability of a drug molecule requires its effective delivery to the target site. In general, majority of synthetically developed molecular entities have high hydrophobic nature as well as low bioavailability, therefore the need for suitable delivery vehicles arises. Self-assembled structures such as micelles, niosomes, and liposomes have been used as effective delivery vehicles and studied extensively. However, the information available in literature is mostly qualitative in nature. We have quantitatively investigated the partitioning of antibiotic drug streptomycin into cationic, nonionic, and a mixture of cationic and nonionic surfactant micelles and its interaction with the transport protein serum albumin upon subsequent delivery. A combination of calorimetry and spectroscopy has been used to obtain the thermodynamic signatures associated with partitioning and interaction with the protein and the resulting conformational changes in the latter. The results have been correlated with other class of drugs of different nature to understand the role of molecular features in the partitioning process. These studies are oriented toward understanding the physical chemistry of partitioning of a variety of drug molecules into suitable delivery vehicles and hence establishing structure-property-energetics relationships. Such studies provide general guidelines toward a broader goal of rational drug design.

  • Mode of action of betaine on some amino acids and globular proteins: Thermodynamic considerations
    Anu A. Thoppil, Eva Judy, and Nand Kishore
    Elsevier BV
    Abstract The interactions of the amino acids glycine, l -alanine, dl -α-amino-n-butyric acid, l -valine, and l -leucine have been studied based on values of apparent molar volume (V2,m,ϕ) and apparent molar compressibility ( K s , 2 , m , ϕ ) in 1 mol·kg−1 and 2 mol·kg−1 aqueous betaine solutions at T = 298.15 K. These thermodynamic quantities have been calculated from density and sound velocity measurements. Isothermal titration calorimetry has been employed to determine the values of enthalpies of interaction of aqueous solutions of these amino acids with betaine. These data have been further used to calculate values of infinite dilution standard partial molar volumes ( V 2 , m o ) , standard partial molar isentropic compressibilities ( K s , 2 , m o ) and limiting enthalpies of dilution ( Δ dil H m o ) of these amino acids in aqueous betaine solutions. The standard partial molar volumes of transfer ( Δ tr V 2 , m o ) , isentropic compressibilities of transfer ( Δ tr K s , 2 , m o ) and enthalpies of dilution of transfer Δtr(ΔdilHom) of amino acids from water to aqueous betaine solutions have been calculated from the measured data in order to understand possible intermolecular interactions such as ion-ion, ion-polar, hydrophilic-hydrophobic and hydrophobic-hydrophobic group interactions. The contributions of the end groups {(NH3+, COO−), CH2 groups and the other alkyl chains of the amino acids to V 2 , m o } have also been determined. The interactions of betaine with the globular proteins α-lactalbumin and bovine serum albumin have also been studied. Such studies are important in obtaining information on the action of osmolytes on proteins and their constituents and establishing possible correlations.

RECENT SCHOLAR PUBLICATIONS

  • Analytical Aspects of ANSA–BSA Association: A Thermodynamic and Conformational Approach
    A Jain, E Judy, N Kishore
    The Journal of Physical Chemistry B 128 (22), 5344-5362 2024

  • Role of water structural properties in interaction of amino acids with metal ions of varying size and electrons in d-block or main group elements: Quantitative thermodynamic
    E Judy, N Kishore
    Journal of Molecular Structure 1294, 136401 2023

  • Prevention of insulin fibrillation by biocompatible choline-amino acid based ionic liquids: Biophysical insights
    E Judy, N Kishore
    Biochimie 207, 20-32 2023

  • Correlating the Properties of Antibiotics with the Energetics of Partitioning in Colloidal Self-Assemblies and the Effect on the Binding of a Released Drug with a Target Protein
    E Judy, N Kishore
    Langmuir 37 (23), 7203-7218 2021

  • Biophysical insights into drug encapsulation and release from self assemblies protein folding intermediates stabilization and prevention of aggregation fibrillation
    E Judy
    Indian Institute of Technology Mumbai 2021

  • Discrepancies in Thermodynamic Information Obtained from Calorimetry and Spectroscopy in Ligand Binding Reactions: Implications on Correct Analysis in Systems of Biological
    E Judy, N Kishore
    Bulletin of the Chemical Society of Japan 94 (2), 473-485 2021

  • Quantitative calorimetric evidences into counteraction mechanism of denaturing effect of guanidine hydrochloride by citrulline and betaine
    E Judy, N Kishore
    Journal of Molecular Liquids 323, 114953 2021

  • Mechanistic insights into encapsulation and release of drugs in colloidal niosomal systems: biophysical aspects
    E Judy, M Lopus, N Kishore
    RSC Advances 11 (56), 35110-35126 2021

  • Partitioning of anticancer drug 5-fluorouracil in micellar media explored by physicochemical properties and energetics of interactions: Quantitative insights for implications
    M Dasgupta, E Judy, N Kishore
    Colloids and Surfaces B: Biointerfaces 187, 110730 2020

  • Thermal methods in partitioning and release of anticancer drugs in colloidal nonionic surfactant vesicles niosomes: mechanistic insights
    E Judy, N Kishore
    Proceedings of the twenty second DAE-BRNS symposium on thermal analysis 2020

  • A look back at the molten globule state of proteins: thermodynamic aspects
    E Judy, N Kishore
    Biophysical reviews 11 (3), 365 2019

  • 1, 1, 1, 3, 3, 3-Hexafluoroisopropanol and 2, 2, 2-trifluoroethanol act more effectively on protein in combination than individually: Thermodynamic aspects
    NS Jha, E Judy, N Kishore
    The Journal of Chemical Thermodynamics 121, 39-48 2018

  • Physicochemical properties of L-carnitine in aqueous solution and its interaction with trimethylamine N-oxide, sodium chloride and dextrose: Volumetric and calorimetric insights
    A Arya, E Judy, N Kishore
    The Journal of Chemical Thermodynamics 120, 141-150 2018

  • Drug partitioning in micellar media and its implications in rational drug design: insights with streptomycin
    E Judy, D Pagariya, N Kishore
    Langmuir 34 (11), 3467-3484 2018

  • Mode of action of betaine on some amino acids and globular proteins: Thermodynamic considerations
    AA Thoppil, E Judy, N Kishore
    The Journal of Chemical Thermodynamics 111, 115-128 2017

  • Biological wonders of osmolytes: the need to know more
    E Judy, N Kishore
    Biochem. Anal. Biochem 5 (4), 1-5 2016

  • Rational Drug Design and Future Directions: Thermodynamic Perspective
    E Judy, S Choudhary, N Kishore
    Austin Biomol Open Access 1 (1), 1003 2016

  • Bioenergetics: Open Access
    E Judy, N Kishore
     2016

MOST CITED SCHOLAR PUBLICATIONS

  • A look back at the molten globule state of proteins: thermodynamic aspects
    E Judy, N Kishore
    Biophysical reviews 11 (3), 365 2019
    Citations: 57

  • Mechanistic insights into encapsulation and release of drugs in colloidal niosomal systems: biophysical aspects
    E Judy, M Lopus, N Kishore
    RSC Advances 11 (56), 35110-35126 2021
    Citations: 29

  • Partitioning of anticancer drug 5-fluorouracil in micellar media explored by physicochemical properties and energetics of interactions: Quantitative insights for implications
    M Dasgupta, E Judy, N Kishore
    Colloids and Surfaces B: Biointerfaces 187, 110730 2020
    Citations: 21

  • Biological wonders of osmolytes: the need to know more
    E Judy, N Kishore
    Biochem. Anal. Biochem 5 (4), 1-5 2016
    Citations: 20

  • Drug partitioning in micellar media and its implications in rational drug design: insights with streptomycin
    E Judy, D Pagariya, N Kishore
    Langmuir 34 (11), 3467-3484 2018
    Citations: 17

  • Mode of action of betaine on some amino acids and globular proteins: Thermodynamic considerations
    AA Thoppil, E Judy, N Kishore
    The Journal of Chemical Thermodynamics 111, 115-128 2017
    Citations: 13

  • Correlating the Properties of Antibiotics with the Energetics of Partitioning in Colloidal Self-Assemblies and the Effect on the Binding of a Released Drug with a Target Protein
    E Judy, N Kishore
    Langmuir 37 (23), 7203-7218 2021
    Citations: 9

  • 1, 1, 1, 3, 3, 3-Hexafluoroisopropanol and 2, 2, 2-trifluoroethanol act more effectively on protein in combination than individually: Thermodynamic aspects
    NS Jha, E Judy, N Kishore
    The Journal of Chemical Thermodynamics 121, 39-48 2018
    Citations: 9

  • Prevention of insulin fibrillation by biocompatible choline-amino acid based ionic liquids: Biophysical insights
    E Judy, N Kishore
    Biochimie 207, 20-32 2023
    Citations: 6

  • Analytical Aspects of ANSA–BSA Association: A Thermodynamic and Conformational Approach
    A Jain, E Judy, N Kishore
    The Journal of Physical Chemistry B 128 (22), 5344-5362 2024
    Citations: 4

  • Discrepancies in Thermodynamic Information Obtained from Calorimetry and Spectroscopy in Ligand Binding Reactions: Implications on Correct Analysis in Systems of Biological
    E Judy, N Kishore
    Bulletin of the Chemical Society of Japan 94 (2), 473-485 2021
    Citations: 4

  • Physicochemical properties of L-carnitine in aqueous solution and its interaction with trimethylamine N-oxide, sodium chloride and dextrose: Volumetric and calorimetric insights
    A Arya, E Judy, N Kishore
    The Journal of Chemical Thermodynamics 120, 141-150 2018
    Citations: 2

  • Role of water structural properties in interaction of amino acids with metal ions of varying size and electrons in d-block or main group elements: Quantitative thermodynamic
    E Judy, N Kishore
    Journal of Molecular Structure 1294, 136401 2023
    Citations: 1

  • Rational Drug Design and Future Directions: Thermodynamic Perspective
    E Judy, S Choudhary, N Kishore
    Austin Biomol Open Access 1 (1), 1003 2016
    Citations: 1