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Kakali Bhadra - One of the best experts on this subject based on the ideXlab platform.
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Pharmaceutical efficacy of Harmalol in inhibiting hepatocellular carcinoma
Future Journal of Pharmaceutical Sciences, 2020Co-Authors: Sarita Sarkar, Paromita Bhattacharjee, Tapas Ghosh, Kakali BhadraAbstract:Background Diethylnitrosamine (DEN) promoted by carbon tetrachloride (CCl_4) forms DNA adducts inducing hepatocellular carcinoma (HCC). Plant alkaloid, Harmalol, is being used as a therapeutic agent against HCC due to its accessibility and efficacy by apoptosis and inhibiting proliferation of cancer epithelial cells. Result Seven groups of Swiss albino mice were taken. Different stages of liver tissues and serum from various experimental groups were collected before and after Harmalol treatment. The investigation was carried out by enzyme assay, bilirubin level in the blood, DNA, RNA, normal serum protein of liver tissue, and alpha-feto protein estimation of serum. Gross morphological assessment of liver, histological, and different apoptosis markers viz. p53, caspase3, and cytochrome C expression were analyzed by RT-PCR and Western blot. Harmalol (10 mg/kg B.W. per week, I.P.) for 9 weeks showed a significant reduction in hepatocellular foci, nodules, and carcinoma ultimately retaining the normal morphology. It further induces ROS-dependent apoptosis through mitochondrial cytochrome C release that induces p53 by caspase3 activation. Conclusion The investigation will eventually help to develop more effective chemotherapeutic drugs from the natural source.
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In vitro relationship between serum protein binding to beta-carboline alkaloids: a comparative cytotoxic, spectroscopic and calorimetric assays.
Journal of Biomolecular Structure & Dynamics, 2019Co-Authors: Tapas Ghosh, Sarita Sarkar, Paromita Bhattacharjee, Prateek Pandya, Gopal Chandra Jana, Maidul Hossain, Kakali BhadraAbstract:AbstractThe work highlighted interaction of Harmalol, harmaline and harmine with human serum albumin by biophysical and biochemical assays. Presence of serum protein in the media negatively affects...
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therapeutic role of Harmalol targeting nucleic acids biophysical perspective and in vitro cytotoxicity
Mini-reviews in Medicinal Chemistry, 2017Co-Authors: Sarita Sarkar, Kakali BhadraAbstract:BACKGROUND: Harmalol, a beta carboline alkaloid, shows remarkable importance in the contemporary biomedical research and drug discovery programs. With time, there is emerging interest in search for better anti-cancer drugs of plant origin with high activity and lower toxicity. Most of the chemotherapeutic agents due to their non-specific target and toxicity on active healthy cells, use is often restricted, necessitating search for newer drugs having greater potentiality. OBJECTIVE: The review highlighted the interaction of Harmalol with nucleic acids of different motifs as sole target biomolecules and in vitro cytotoxicity of the alkaloid in human cancer cell lines with special emphasis on its apoptotic induction ability. METHODS: Binding study and in vitro cytotoxicity was performed using several biophysical techniques and biochemical assays, respectively. RESULTS: Data from competition dialysis, UV and fluorescence spectroscopic analysis, circular dichroism, viscometry and isothermal calorimetry shows binding and interaction of Harmalol with several natural and synthetic nucleic acids, both DNA and RNA, of different motifs. Furthermore, apoptotic hallmarks like internucleosomal DNA fragmentation, membrane blebbing, cell shrinkage, chromatin condensation, change of mitochondrial membrane potential, comet tail formation and ROS (reactive oxygen species) dependent cytotoxicity being analyzed in the Harmalol treated cancer cells. CONCLUSION: These results stating the therapeutic role of Harmalol, will lead to the interesting knowledge on the cytotoxicity, mode, mechanism, specificity of binding and correlation between structural aspects and energetics enabling a complete set of guidelines for design of new drugs.
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dna binding and apoptotic induction ability of Harmalol in hepg2 biophysical and biochemical approaches
Chemico-Biological Interactions, 2016Co-Authors: Sarita Sarkar, Paromita Bhattacharjee, Kakali BhadraAbstract:Abstract Harmalol administration caused remarkable reduction in proliferation of HepG2 cells with GI50 of 14.2 μM, without showing much cytotoxicity in embryonic liver cell line, WRL-68. Data from circular dichroism (CD) and differential scanning calorimetric (DSC) analysis of Harmalol-CT DNA complex shows conformational changes with prominent CD perturbation and stabilization of CT DNA by 8 °C. Binding constant and stoichiometry was calculated using the above biophysical techniques. The Scatchard plot constructed from CD data showed cooperative binding, from which the cooperative binding affinity (K’ω) of 4.65 ± 0.7 × 105 M−1, and n value of 4.16 were deduced. The binding parameter obtained from DSC melting data was in good agreement with the above CD data. Furthermore, dose dependent apoptotic induction ability of Harmalol was studied in HepG2 cells using different biochemical assays. Generation of ROS, DNA damage, changes in cellular external and ultramorphology, alteration of membrane, formation of comet tail, decreased mitochondrial membrane potential and a significant increase in Sub Go/G1 population made the cancer cell, HepG2, prone to apoptosis. Up regulation of p53 and caspase 3 further indicated the apoptotic role of Harmalol.
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targeting different rna motifs by beta carboline alkaloid Harmalol a comparative photophysical calorimetric and molecular docking approach
Journal of Biomolecular Structure & Dynamics, 2016Co-Authors: Paromita Bhattacharjee, Sarita Sarkar, Prateek Pandya, Kakali BhadraAbstract:AbstractRNA has attracted recent attention for its key role in gene expression and targeting by small molecules for therapeutic intervention. This work focuses towards understanding interaction of Harmalol, a DNA intercalator, with RNAs of different motifs viz. single-stranded A-form poly(A), double-stranded A-form of poly(C)·poly(G), and clover leaf tRNAphe by different spectroscopic, calorimetric, and molecular modeling techniques. Results of this study converge to suggest that (i) binding constant varied in the order poly(C)·poly(G) > tRNAphe > poly(A), (ii) non-cooperative binding of Harmalol to poly(C)·poly(G) and poly(A) and cooperative binding with tRNAphe, (iii) significant structural changes of poly(C)·poly(G) and tRNAphe with concomitant induction of optical activity in the bound achiral alkaloid molecules, while with poly(A) no induced Circular dichroism (CD) perturbation was observed, (iv) the binding was predominantly exothermic, enthalpy-driven, entropy-favored with poly(C)·poly(G), while it...
Sarita Sarkar - One of the best experts on this subject based on the ideXlab platform.
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Pharmaceutical efficacy of Harmalol in inhibiting hepatocellular carcinoma
Future Journal of Pharmaceutical Sciences, 2020Co-Authors: Sarita Sarkar, Paromita Bhattacharjee, Tapas Ghosh, Kakali BhadraAbstract:Background Diethylnitrosamine (DEN) promoted by carbon tetrachloride (CCl_4) forms DNA adducts inducing hepatocellular carcinoma (HCC). Plant alkaloid, Harmalol, is being used as a therapeutic agent against HCC due to its accessibility and efficacy by apoptosis and inhibiting proliferation of cancer epithelial cells. Result Seven groups of Swiss albino mice were taken. Different stages of liver tissues and serum from various experimental groups were collected before and after Harmalol treatment. The investigation was carried out by enzyme assay, bilirubin level in the blood, DNA, RNA, normal serum protein of liver tissue, and alpha-feto protein estimation of serum. Gross morphological assessment of liver, histological, and different apoptosis markers viz. p53, caspase3, and cytochrome C expression were analyzed by RT-PCR and Western blot. Harmalol (10 mg/kg B.W. per week, I.P.) for 9 weeks showed a significant reduction in hepatocellular foci, nodules, and carcinoma ultimately retaining the normal morphology. It further induces ROS-dependent apoptosis through mitochondrial cytochrome C release that induces p53 by caspase3 activation. Conclusion The investigation will eventually help to develop more effective chemotherapeutic drugs from the natural source.
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In vitro relationship between serum protein binding to beta-carboline alkaloids: a comparative cytotoxic, spectroscopic and calorimetric assays.
Journal of Biomolecular Structure & Dynamics, 2019Co-Authors: Tapas Ghosh, Sarita Sarkar, Paromita Bhattacharjee, Prateek Pandya, Gopal Chandra Jana, Maidul Hossain, Kakali BhadraAbstract:AbstractThe work highlighted interaction of Harmalol, harmaline and harmine with human serum albumin by biophysical and biochemical assays. Presence of serum protein in the media negatively affects...
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therapeutic role of Harmalol targeting nucleic acids biophysical perspective and in vitro cytotoxicity
Mini-reviews in Medicinal Chemistry, 2017Co-Authors: Sarita Sarkar, Kakali BhadraAbstract:BACKGROUND: Harmalol, a beta carboline alkaloid, shows remarkable importance in the contemporary biomedical research and drug discovery programs. With time, there is emerging interest in search for better anti-cancer drugs of plant origin with high activity and lower toxicity. Most of the chemotherapeutic agents due to their non-specific target and toxicity on active healthy cells, use is often restricted, necessitating search for newer drugs having greater potentiality. OBJECTIVE: The review highlighted the interaction of Harmalol with nucleic acids of different motifs as sole target biomolecules and in vitro cytotoxicity of the alkaloid in human cancer cell lines with special emphasis on its apoptotic induction ability. METHODS: Binding study and in vitro cytotoxicity was performed using several biophysical techniques and biochemical assays, respectively. RESULTS: Data from competition dialysis, UV and fluorescence spectroscopic analysis, circular dichroism, viscometry and isothermal calorimetry shows binding and interaction of Harmalol with several natural and synthetic nucleic acids, both DNA and RNA, of different motifs. Furthermore, apoptotic hallmarks like internucleosomal DNA fragmentation, membrane blebbing, cell shrinkage, chromatin condensation, change of mitochondrial membrane potential, comet tail formation and ROS (reactive oxygen species) dependent cytotoxicity being analyzed in the Harmalol treated cancer cells. CONCLUSION: These results stating the therapeutic role of Harmalol, will lead to the interesting knowledge on the cytotoxicity, mode, mechanism, specificity of binding and correlation between structural aspects and energetics enabling a complete set of guidelines for design of new drugs.
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dna binding and apoptotic induction ability of Harmalol in hepg2 biophysical and biochemical approaches
Chemico-Biological Interactions, 2016Co-Authors: Sarita Sarkar, Paromita Bhattacharjee, Kakali BhadraAbstract:Abstract Harmalol administration caused remarkable reduction in proliferation of HepG2 cells with GI50 of 14.2 μM, without showing much cytotoxicity in embryonic liver cell line, WRL-68. Data from circular dichroism (CD) and differential scanning calorimetric (DSC) analysis of Harmalol-CT DNA complex shows conformational changes with prominent CD perturbation and stabilization of CT DNA by 8 °C. Binding constant and stoichiometry was calculated using the above biophysical techniques. The Scatchard plot constructed from CD data showed cooperative binding, from which the cooperative binding affinity (K’ω) of 4.65 ± 0.7 × 105 M−1, and n value of 4.16 were deduced. The binding parameter obtained from DSC melting data was in good agreement with the above CD data. Furthermore, dose dependent apoptotic induction ability of Harmalol was studied in HepG2 cells using different biochemical assays. Generation of ROS, DNA damage, changes in cellular external and ultramorphology, alteration of membrane, formation of comet tail, decreased mitochondrial membrane potential and a significant increase in Sub Go/G1 population made the cancer cell, HepG2, prone to apoptosis. Up regulation of p53 and caspase 3 further indicated the apoptotic role of Harmalol.
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targeting different rna motifs by beta carboline alkaloid Harmalol a comparative photophysical calorimetric and molecular docking approach
Journal of Biomolecular Structure & Dynamics, 2016Co-Authors: Paromita Bhattacharjee, Sarita Sarkar, Prateek Pandya, Kakali BhadraAbstract:AbstractRNA has attracted recent attention for its key role in gene expression and targeting by small molecules for therapeutic intervention. This work focuses towards understanding interaction of Harmalol, a DNA intercalator, with RNAs of different motifs viz. single-stranded A-form poly(A), double-stranded A-form of poly(C)·poly(G), and clover leaf tRNAphe by different spectroscopic, calorimetric, and molecular modeling techniques. Results of this study converge to suggest that (i) binding constant varied in the order poly(C)·poly(G) > tRNAphe > poly(A), (ii) non-cooperative binding of Harmalol to poly(C)·poly(G) and poly(A) and cooperative binding with tRNAphe, (iii) significant structural changes of poly(C)·poly(G) and tRNAphe with concomitant induction of optical activity in the bound achiral alkaloid molecules, while with poly(A) no induced Circular dichroism (CD) perturbation was observed, (iv) the binding was predominantly exothermic, enthalpy-driven, entropy-favored with poly(C)·poly(G), while it...
Bahram Hemmateenejad - One of the best experts on this subject based on the ideXlab platform.
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combined fluorescence spectroscopy and molecular modeling studies on the interaction between Harmalol and human serum albumin
Journal of Pharmaceutical and Biomedical Analysis, 2012Co-Authors: Bahram Hemmateenejad, Mojtaba Shamsipur, Fayezeh Samari, Taghi Khayamian, Malihe Ebrahimi, Zahra RezaeiAbstract:Abstract The interaction between Harmalol and human serum albumin (HSA) has been studied by fluorescence spectroscopy and molecular modeling methods. The intrinsic fluorescence of HSA was quenched by Harmalol, which was rationalized in terms of the static quenching mechanism. The binding parameters, quenching constants and conformation changes were determined by fluorescence quenching method. The thermodynamic parameters, calculated from the temperature dependence of binding constants (i.e., Δ H ° = −62.7 kJ mol −1 and Δ S ° = −119.3 J mol −1 K −1 ), indicated the major role of van der Waals force and hydrogen bonding in binding process. Site marker competitive experiments revealed that Harmalol binds to both the IIA and IIIA sub-domains of HSA with a slight preference toward sub-domain IIA. Finally, the binding of Harmalol to HSA was modeled by molecular docking and molecular dynamic simulation methods. Excellent agreement was found between the experimental and theoretical results with respect to the mechanism of binding and binding constants. Molecular dynamic simulation revealed that HSA does not have a significant conformational change when it binds with Harmalol.
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partial least squares based multivariate spectral calibration method for simultaneous determination of beta carboline derivatives in peganum harmala seed extracts
Analytica Chimica Acta, 2006Co-Authors: Bahram Hemmateenejad, Abdolkarim Abbaspour, Homeyra Maghami, Ramin Miri, Mohhamad Reza PanjehshahinAbstract:Abstract The partial least squares regression method has been applied for simultaneous spectrophotometric determination of harmine, harmane, Harmalol and harmaline in Peganum harmala L. (Zygophyllaceae) seeds. The effect of pH was optimized employing multivariate definition of selectivity and sensitivity and best results were obtained in basic media (pH > 9). The calibration models were optimized for number of latent variables by the cross-validation procedure. Determinations were made over the concentration range of 0.15–10 μg mL −1 . The proposed method was validated by applying it to the analysis of the β-carbolines in synthetic quaternary mixtures of media at pH 9 and 11. The relative standard errors of prediction were less than 4% in most cases. Analysis of P. harmala seeds by the proposed models for contents of the β-carboline derivatives resulted in 1.84%, 0.16%, 0.25% and 3.90% for harmine, harmane, harmaline and Harmalol, respectively. The results were validated against an existing HPLC method and it no significant differences were observed between the results of two methods.
Yoon Young Jang - One of the best experts on this subject based on the ideXlab platform.
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protective effect of Harmalol and harmaline on mptp neurotoxicity in the mouse and dopamine induced damage of brain mitochondria and pc12 cells
Journal of Neurochemistry, 2002Co-Authors: Yoon Young Jang, Hyun Wook HaAbstract:The present study elucidated the protective effect of β-carbolines (harmaline, Harmalol, and harmine) on oxidative neuronal damage. MPTP treatment increased activities of total superoxide dismutase, catalase, and glutathione peroxidase and levels of malondialdehyde and carbonyls in the basal ganglia, diencephalon plus midbrain of brain compared with control mouse brain. Coadministration of Harmalol (48 mg/kg) attenuated the MPTP effect on the enzyme activities and formation of tissue peroxidation products. Harmaline, Harmalol, and harmine attenuated both the 500 μM MPP+-induced inhibition of electron flow and membrane potential formation and the 100 μM dopamine-induced thiol oxidation and carbonyl formation in mitochondria. The scavenging action of β-carbolines on hydroxyl radicals was represented by inhibition of 2-deoxy-d-ribose degradation. Harmaline and Harmalol (100 μM) attenuated 200 μM dopamine-induced viability loss in PC12 cells. The β-carbolines (50 μM) attenuated 50 μM dopamine-induced apoptosis in PC12 cells. The compounds alone did not exhibit significant cytotoxic effects. The results indicate that β-carbolines attenuate brain damage in mice treated with MPTP and MPP+-induced mitochondrial damage. The compounds may prevent dopamine-induced mitochondrial damage and PC12 cell death through a scavenging action on reactive oxygen species and inhibition of monoamine oxidase and thiol oxidation.
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Protective effect of harmaline and Harmalol against dopamine‐ and 6‐hydroxydopamine‐induced oxidative damage of brain mitochondria and synaptosomes, and viability loss of PC12 cells
European Journal of Neuroscience, 2001Co-Authors: Yoon Young JangAbstract:: The present study elucidated the protective effect of beta-carbolines (harmaline, Harmalol and harmine) against oxidative damage of brain mitochondria, synaptosomes and PC12 cells induced by either dopamine or 6-hydroxydopamine. Harmaline, Harmalol and antioxidant enzymes (superoxide dismutase/SOD and catalase) decreased the alteration of mitochondrial swelling and membrane potential induced by 200 microM dopamine or 100 microM 6-hydroxydopamine. Deprenyl attenuated the dopamine-induced mitochondrial dysfunction but did not reduce the effect of 6-hydroxydopamine. While beta-carbolines inhibited the electron flow in mitochondria, they did not enhance the depressant effect of catecholamines. beta-Carbolines and antioxidant enzymes reversed the depression of synaptosomal Ca2+ uptake induced by 10 microM catecholamines. The compounds inhibited the catecholamine-induced thioredoxin reductase inhibition, thiol oxidation and carbonyl formation in mitochondria and synaptosomes. beta-Carbolines decreased the reactive species-induced deoxyribose degradation. Harmaline and Harmalol reduced the catecholamine-induced loss of the transmembrane potential and of cell viability in PC12 cells. beta-Carbolines alone did not show a significant cytotoxic effect on PC12 cells. The results suggest that beta-carbolines may attenuate the dopamine- or 6-hydroxydopamine-induced alteration of brain mitochondrial and synaptosomal functions, and viability loss in PC12 cells, by a scavenging action on reactive oxygen species and inhibition of thiol oxidation.
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protective effect of harmaline and Harmalol against dopamine and 6 hydroxydopamine induced oxidative damage of brain mitochondria and synaptosomes and viability loss of pc12 cells
European Journal of Neuroscience, 2001Co-Authors: Yoon Young JangAbstract:: The present study elucidated the protective effect of beta-carbolines (harmaline, Harmalol and harmine) against oxidative damage of brain mitochondria, synaptosomes and PC12 cells induced by either dopamine or 6-hydroxydopamine. Harmaline, Harmalol and antioxidant enzymes (superoxide dismutase/SOD and catalase) decreased the alteration of mitochondrial swelling and membrane potential induced by 200 microM dopamine or 100 microM 6-hydroxydopamine. Deprenyl attenuated the dopamine-induced mitochondrial dysfunction but did not reduce the effect of 6-hydroxydopamine. While beta-carbolines inhibited the electron flow in mitochondria, they did not enhance the depressant effect of catecholamines. beta-Carbolines and antioxidant enzymes reversed the depression of synaptosomal Ca2+ uptake induced by 10 microM catecholamines. The compounds inhibited the catecholamine-induced thioredoxin reductase inhibition, thiol oxidation and carbonyl formation in mitochondria and synaptosomes. beta-Carbolines decreased the reactive species-induced deoxyribose degradation. Harmaline and Harmalol reduced the catecholamine-induced loss of the transmembrane potential and of cell viability in PC12 cells. beta-Carbolines alone did not show a significant cytotoxic effect on PC12 cells. The results suggest that beta-carbolines may attenuate the dopamine- or 6-hydroxydopamine-induced alteration of brain mitochondrial and synaptosomal functions, and viability loss in PC12 cells, by a scavenging action on reactive oxygen species and inhibition of thiol oxidation.
Paromita Bhattacharjee - One of the best experts on this subject based on the ideXlab platform.
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Pharmaceutical efficacy of Harmalol in inhibiting hepatocellular carcinoma
Future Journal of Pharmaceutical Sciences, 2020Co-Authors: Sarita Sarkar, Paromita Bhattacharjee, Tapas Ghosh, Kakali BhadraAbstract:Background Diethylnitrosamine (DEN) promoted by carbon tetrachloride (CCl_4) forms DNA adducts inducing hepatocellular carcinoma (HCC). Plant alkaloid, Harmalol, is being used as a therapeutic agent against HCC due to its accessibility and efficacy by apoptosis and inhibiting proliferation of cancer epithelial cells. Result Seven groups of Swiss albino mice were taken. Different stages of liver tissues and serum from various experimental groups were collected before and after Harmalol treatment. The investigation was carried out by enzyme assay, bilirubin level in the blood, DNA, RNA, normal serum protein of liver tissue, and alpha-feto protein estimation of serum. Gross morphological assessment of liver, histological, and different apoptosis markers viz. p53, caspase3, and cytochrome C expression were analyzed by RT-PCR and Western blot. Harmalol (10 mg/kg B.W. per week, I.P.) for 9 weeks showed a significant reduction in hepatocellular foci, nodules, and carcinoma ultimately retaining the normal morphology. It further induces ROS-dependent apoptosis through mitochondrial cytochrome C release that induces p53 by caspase3 activation. Conclusion The investigation will eventually help to develop more effective chemotherapeutic drugs from the natural source.
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In vitro relationship between serum protein binding to beta-carboline alkaloids: a comparative cytotoxic, spectroscopic and calorimetric assays.
Journal of Biomolecular Structure & Dynamics, 2019Co-Authors: Tapas Ghosh, Sarita Sarkar, Paromita Bhattacharjee, Prateek Pandya, Gopal Chandra Jana, Maidul Hossain, Kakali BhadraAbstract:AbstractThe work highlighted interaction of Harmalol, harmaline and harmine with human serum albumin by biophysical and biochemical assays. Presence of serum protein in the media negatively affects...
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dna binding and apoptotic induction ability of Harmalol in hepg2 biophysical and biochemical approaches
Chemico-Biological Interactions, 2016Co-Authors: Sarita Sarkar, Paromita Bhattacharjee, Kakali BhadraAbstract:Abstract Harmalol administration caused remarkable reduction in proliferation of HepG2 cells with GI50 of 14.2 μM, without showing much cytotoxicity in embryonic liver cell line, WRL-68. Data from circular dichroism (CD) and differential scanning calorimetric (DSC) analysis of Harmalol-CT DNA complex shows conformational changes with prominent CD perturbation and stabilization of CT DNA by 8 °C. Binding constant and stoichiometry was calculated using the above biophysical techniques. The Scatchard plot constructed from CD data showed cooperative binding, from which the cooperative binding affinity (K’ω) of 4.65 ± 0.7 × 105 M−1, and n value of 4.16 were deduced. The binding parameter obtained from DSC melting data was in good agreement with the above CD data. Furthermore, dose dependent apoptotic induction ability of Harmalol was studied in HepG2 cells using different biochemical assays. Generation of ROS, DNA damage, changes in cellular external and ultramorphology, alteration of membrane, formation of comet tail, decreased mitochondrial membrane potential and a significant increase in Sub Go/G1 population made the cancer cell, HepG2, prone to apoptosis. Up regulation of p53 and caspase 3 further indicated the apoptotic role of Harmalol.
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targeting different rna motifs by beta carboline alkaloid Harmalol a comparative photophysical calorimetric and molecular docking approach
Journal of Biomolecular Structure & Dynamics, 2016Co-Authors: Paromita Bhattacharjee, Sarita Sarkar, Prateek Pandya, Kakali BhadraAbstract:AbstractRNA has attracted recent attention for its key role in gene expression and targeting by small molecules for therapeutic intervention. This work focuses towards understanding interaction of Harmalol, a DNA intercalator, with RNAs of different motifs viz. single-stranded A-form poly(A), double-stranded A-form of poly(C)·poly(G), and clover leaf tRNAphe by different spectroscopic, calorimetric, and molecular modeling techniques. Results of this study converge to suggest that (i) binding constant varied in the order poly(C)·poly(G) > tRNAphe > poly(A), (ii) non-cooperative binding of Harmalol to poly(C)·poly(G) and poly(A) and cooperative binding with tRNAphe, (iii) significant structural changes of poly(C)·poly(G) and tRNAphe with concomitant induction of optical activity in the bound achiral alkaloid molecules, while with poly(A) no induced Circular dichroism (CD) perturbation was observed, (iv) the binding was predominantly exothermic, enthalpy-driven, entropy-favored with poly(C)·poly(G), while it...
