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Rajagopal Subramanyam - One of the best experts on this subject based on the ideXlab platform.
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molecular dynamics simulation and binding studies of β Sitosterol with human serum albumin and its biological relevance
Journal of Physical Chemistry B, 2010Co-Authors: Babu Sudhamalla, Mahesh Gokara, Navjeet Ahalawat, Damu G Amooru, Rajagopal SubramanyamAbstract:β-Sitosterol is a naturally occurring phytosterol that is widely used to cure atherosclerosis, diabetes, cancer, and inflammation and is also an antioxidant. Here, we studied the interaction of β-Sitosterol, isolated from the aerial roots of Ficus bengalensis, with human serum albumin (HSA) at physiological pH 7.2 by using fluorescence, circular dichroism (CD), molecular docking, and molecular dynamics simulation methods. The experimental results show that the intrinsic fluorescence of HSA is quenched by addition of β-Sitosterol through a static quenching mechanism. The binding constant of the compound to HSA, calculated from fluorescence data, was found to be Kβ-Sitosterol = 4.6 ± 0.01 × 103 M−1, which corresponds to −5.0 kcal M−1 of free energy. Upon binding of β-Sitosterol to HSA, the protein secondary structure was partially unfolded. Specifically, the molecular dynamics study makes an important contribution to understanding the effect of the binding of β-Sitosterol on conformational changes of HSA an...
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molecular dynamics simulation and binding studies of β Sitosterol with human serum albumin and its biological relevance
Journal of Physical Chemistry B, 2010Co-Authors: Babu Sudhamalla, Mahesh Gokara, Navjeet Ahalawat, Damu G Amooru, Rajagopal SubramanyamAbstract:Beta-Sitosterol is a naturally occurring phytosterol that is widely used to cure atherosclerosis, diabetes, cancer, and inflammation and is also an antioxidant. Here, we studied the interaction of beta-Sitosterol, isolated from the aerial roots of Ficus bengalensis, with human serum albumin (HSA) at physiological pH 7.2 by using fluorescence, circular dichroism (CD), molecular docking, and molecular dynamics simulation methods. The experimental results show that the intrinsic fluorescence of HSA is quenched by addition of beta-Sitosterol through a static quenching mechanism. The binding constant of the compound to HSA, calculated from fluorescence data, was found to be K(beta-Sitosterol) = 4.6 +/- 0.01 x 10(3) M(-1), which corresponds to -5.0 kcal M(-1) of free energy. Upon binding of beta-Sitosterol to HSA, the protein secondary structure was partially unfolded. Specifically, the molecular dynamics study makes an important contribution to understanding the effect of the binding of beta-Sitosterol on conformational changes of HSA and the stability of a protein-drug complex system in aqueous solution. Molecular docking studies revealed that the beta-Sitosterol can bind in the large hydrophobic cavity of subdomain IIA, mainly by the hydrophobic interaction but also by hydrogen bond interactions between the hydroxyl (OH) group of carbon-3 of beta-Sitosterol to Arg(257), Ser(287), and Ala(261) of HSA, with hydrogen bond distances of 1.9, 2.4, and 2.2 A, respectively.
Navjeet Ahalawat - One of the best experts on this subject based on the ideXlab platform.
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molecular dynamics simulation and binding studies of β Sitosterol with human serum albumin and its biological relevance
Journal of Physical Chemistry B, 2010Co-Authors: Babu Sudhamalla, Mahesh Gokara, Navjeet Ahalawat, Damu G Amooru, Rajagopal SubramanyamAbstract:β-Sitosterol is a naturally occurring phytosterol that is widely used to cure atherosclerosis, diabetes, cancer, and inflammation and is also an antioxidant. Here, we studied the interaction of β-Sitosterol, isolated from the aerial roots of Ficus bengalensis, with human serum albumin (HSA) at physiological pH 7.2 by using fluorescence, circular dichroism (CD), molecular docking, and molecular dynamics simulation methods. The experimental results show that the intrinsic fluorescence of HSA is quenched by addition of β-Sitosterol through a static quenching mechanism. The binding constant of the compound to HSA, calculated from fluorescence data, was found to be Kβ-Sitosterol = 4.6 ± 0.01 × 103 M−1, which corresponds to −5.0 kcal M−1 of free energy. Upon binding of β-Sitosterol to HSA, the protein secondary structure was partially unfolded. Specifically, the molecular dynamics study makes an important contribution to understanding the effect of the binding of β-Sitosterol on conformational changes of HSA an...
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molecular dynamics simulation and binding studies of β Sitosterol with human serum albumin and its biological relevance
Journal of Physical Chemistry B, 2010Co-Authors: Babu Sudhamalla, Mahesh Gokara, Navjeet Ahalawat, Damu G Amooru, Rajagopal SubramanyamAbstract:Beta-Sitosterol is a naturally occurring phytosterol that is widely used to cure atherosclerosis, diabetes, cancer, and inflammation and is also an antioxidant. Here, we studied the interaction of beta-Sitosterol, isolated from the aerial roots of Ficus bengalensis, with human serum albumin (HSA) at physiological pH 7.2 by using fluorescence, circular dichroism (CD), molecular docking, and molecular dynamics simulation methods. The experimental results show that the intrinsic fluorescence of HSA is quenched by addition of beta-Sitosterol through a static quenching mechanism. The binding constant of the compound to HSA, calculated from fluorescence data, was found to be K(beta-Sitosterol) = 4.6 +/- 0.01 x 10(3) M(-1), which corresponds to -5.0 kcal M(-1) of free energy. Upon binding of beta-Sitosterol to HSA, the protein secondary structure was partially unfolded. Specifically, the molecular dynamics study makes an important contribution to understanding the effect of the binding of beta-Sitosterol on conformational changes of HSA and the stability of a protein-drug complex system in aqueous solution. Molecular docking studies revealed that the beta-Sitosterol can bind in the large hydrophobic cavity of subdomain IIA, mainly by the hydrophobic interaction but also by hydrogen bond interactions between the hydroxyl (OH) group of carbon-3 of beta-Sitosterol to Arg(257), Ser(287), and Ala(261) of HSA, with hydrogen bond distances of 1.9, 2.4, and 2.2 A, respectively.
Ashfaq Ahmad - One of the best experts on this subject based on the ideXlab platform.
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anti alzheimer s studies on β Sitosterol isolated from polygonum hydropiper l
Frontiers in Pharmacology, 2017Co-Authors: Muhammad Ayaz, Farhat Ullah, Abdul Sadiq, Muhammad Ovais, Fazal Subhan, Muhammad Junaid, Muhammad Shahid, Ashfaq AhmadAbstract:The family Polygonaceae is known for its traditional use in the management of various neurological disorders including Alzheimer disease (AD). In search of new anti-AD drugs, β-Sitosterol isolated from Polygonum hydropiper was subjected to in vitro, in vivo, behavioral and molecular docking studies to confirm its possibility as a potential anti-Alzheimer’s agent. The in vitro AChE, BChE inhibitory potentials of β-Sitosterol were investigated following Ellman's assay. The antioxidant activity was tested using DPPH, ABTS and H2O2 assays. Behavioral studies were performed on a sub-strain of transgenic mice using shallow water maze (SWM), Y-maze and balance beam tests. β-Sitosterol was tested for in vivo inhibitory potentials against cholinesterase's and free radicals in the frontal cortex (FC) and hippocampus (HC). The molecular docking study was performed to predict the binding mode of β-Sitosterol in the active sites of AChE and BChE as inhibitor. Considerable in vitro and in vivo cholinesterase inhibitory effects were observed in the β-Sitosterol treated groups. β-Sitosterol exhibited an IC50 value of 55 and 50 µg/ml against AChE and BChE respectively. Whereas, the activity of these enzymes were significantly low in FC and HC homogenates of transgenic animals. Molecular docking studies also support the binding of β-Sitosterol with the target enzyme and further support the in vitro and in vivo results. In the antioxidant assays, the IC50 values were observed as 140, 120 and 280 µg/ml in the DPPH, ABTS and H2O2 assays respectively. The free radicals load in the brain tissues was significantly declined in the β-Sitosterol treated animals as compared to the transgenic-saline treated groups. In the memory assessment and coordination tasks including SWM, Y-maze and balance beam tests, β-Sitosterol treated transgenic animals showed gradual improvement in working memory, spontaneous alternation behavior and motor coordination. These results conclude that β-Sitosterol is a potential compound for the management of memory deficit disorders like AD.
Deborah Echegoyen - One of the best experts on this subject based on the ideXlab platform.
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Bioactivity studies on β‐Sitosterol and its glucoside
Phytotherapy Research, 2002Co-Authors: Irene M Villasenor, Jennifer S Angelada, Arlyn P Canlas, Deborah EchegoyenAbstract:β-Sitosterol and β-sitosteryl-β-D-glucoside were isolated as analgesic constituents from the leaves of Mentha cordifolia Opiz. The acetic acid-induced writhing test showed that β-Sitosterol and β-sitosteryl-β-D-glucoside decreased the number of squirms induced by acetic acid by 70.0% and 73.0%, respectively, at a dose of 100 mg / kg mouse. Statistical analysis using the Kruskall Wallis one-way analysis of variance by ranks showed that these isolates approximate the analgesic activity of mefenamic acid at a 0.001 level of significance. The hot plate method confirmed their analgesic activities, as β-Sitosterol and β-sitosteryl-β-D-glucoside exhibited a 300% and 157% increase in pain tolerance, respectively, while mefenamic acid, a known analgesic, showed a 171% increase. Neither isolate exhibited antiinflammatory activity using the carrageenan-induced mouse paw oedema assay. β-Sitosterol also exhibited anthelminthic and antimutagenic activities. In vitro tests using live Ascaris suum as test animals showed that the behaviour of worms treated with β-Sitosterol approximated that of the positive controls, Combantrin and Antiox. An in vivo micronucleus test showed that β-Sitosterol inhibited the mutagenicity of tetracycline by 65.3% at a dose of 0.5 mg /kg mouse. At the same dose, it did not exhibit chromosome-breaking activity. Copyright © 2002 John Wiley & Sons, Ltd.
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bioactivity studies on β Sitosterol and its glucoside
Phytotherapy Research, 2002Co-Authors: Irene M Villasenor, Jennifer S Angelada, Arlyn P Canlas, Deborah EchegoyenAbstract:β-Sitosterol and β-sitosteryl-β-D-glucoside were isolated as analgesic constituents from the leaves of Mentha cordifolia Opiz. The acetic acid-induced writhing test showed that β-Sitosterol and β-sitosteryl-β-D-glucoside decreased the number of squirms induced by acetic acid by 70.0% and 73.0%, respectively, at a dose of 100 mg / kg mouse. Statistical analysis using the Kruskall Wallis one-way analysis of variance by ranks showed that these isolates approximate the analgesic activity of mefenamic acid at a 0.001 level of significance. The hot plate method confirmed their analgesic activities, as β-Sitosterol and β-sitosteryl-β-D-glucoside exhibited a 300% and 157% increase in pain tolerance, respectively, while mefenamic acid, a known analgesic, showed a 171% increase. Neither isolate exhibited antiinflammatory activity using the carrageenan-induced mouse paw oedema assay. β-Sitosterol also exhibited anthelminthic and antimutagenic activities. In vitro tests using live Ascaris suum as test animals showed that the behaviour of worms treated with β-Sitosterol approximated that of the positive controls, Combantrin and Antiox. An in vivo micronucleus test showed that β-Sitosterol inhibited the mutagenicity of tetracycline by 65.3% at a dose of 0.5 mg /kg mouse. At the same dose, it did not exhibit chromosome-breaking activity. Copyright © 2002 John Wiley & Sons, Ltd.
Babu Sudhamalla - One of the best experts on this subject based on the ideXlab platform.
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molecular dynamics simulation and binding studies of β Sitosterol with human serum albumin and its biological relevance
Journal of Physical Chemistry B, 2010Co-Authors: Babu Sudhamalla, Mahesh Gokara, Navjeet Ahalawat, Damu G Amooru, Rajagopal SubramanyamAbstract:β-Sitosterol is a naturally occurring phytosterol that is widely used to cure atherosclerosis, diabetes, cancer, and inflammation and is also an antioxidant. Here, we studied the interaction of β-Sitosterol, isolated from the aerial roots of Ficus bengalensis, with human serum albumin (HSA) at physiological pH 7.2 by using fluorescence, circular dichroism (CD), molecular docking, and molecular dynamics simulation methods. The experimental results show that the intrinsic fluorescence of HSA is quenched by addition of β-Sitosterol through a static quenching mechanism. The binding constant of the compound to HSA, calculated from fluorescence data, was found to be Kβ-Sitosterol = 4.6 ± 0.01 × 103 M−1, which corresponds to −5.0 kcal M−1 of free energy. Upon binding of β-Sitosterol to HSA, the protein secondary structure was partially unfolded. Specifically, the molecular dynamics study makes an important contribution to understanding the effect of the binding of β-Sitosterol on conformational changes of HSA an...
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molecular dynamics simulation and binding studies of β Sitosterol with human serum albumin and its biological relevance
Journal of Physical Chemistry B, 2010Co-Authors: Babu Sudhamalla, Mahesh Gokara, Navjeet Ahalawat, Damu G Amooru, Rajagopal SubramanyamAbstract:Beta-Sitosterol is a naturally occurring phytosterol that is widely used to cure atherosclerosis, diabetes, cancer, and inflammation and is also an antioxidant. Here, we studied the interaction of beta-Sitosterol, isolated from the aerial roots of Ficus bengalensis, with human serum albumin (HSA) at physiological pH 7.2 by using fluorescence, circular dichroism (CD), molecular docking, and molecular dynamics simulation methods. The experimental results show that the intrinsic fluorescence of HSA is quenched by addition of beta-Sitosterol through a static quenching mechanism. The binding constant of the compound to HSA, calculated from fluorescence data, was found to be K(beta-Sitosterol) = 4.6 +/- 0.01 x 10(3) M(-1), which corresponds to -5.0 kcal M(-1) of free energy. Upon binding of beta-Sitosterol to HSA, the protein secondary structure was partially unfolded. Specifically, the molecular dynamics study makes an important contribution to understanding the effect of the binding of beta-Sitosterol on conformational changes of HSA and the stability of a protein-drug complex system in aqueous solution. Molecular docking studies revealed that the beta-Sitosterol can bind in the large hydrophobic cavity of subdomain IIA, mainly by the hydrophobic interaction but also by hydrogen bond interactions between the hydroxyl (OH) group of carbon-3 of beta-Sitosterol to Arg(257), Ser(287), and Ala(261) of HSA, with hydrogen bond distances of 1.9, 2.4, and 2.2 A, respectively.
