Background: Cheilanthes tenuifolia, a member of the Pteridaceae family, is an evergreen and small fern could be abundant of bioactive compounds. The present study was designed to investigate its many therapeutic properties and isolation of bioactive compounds from extracts of Cheilanthes tenuifolia. Methods: The dried coarse plant powder was extracted with methanol and dried with rotary evaporator. The extract was further partitioned according to the increasing polarity: N-hexane < chloroform < ethyl-acetate < methanol by modified Kupchan method. Then each extract fractions were investigated for their pharmacologic properties. Compounds were isolated from n-hexane fraction through column chromatography, followed by TLC and structure was determined by analysis of sample using 1 H-NMR and matched with published phytochemistry report. Results: Methanol fraction of Cheilanthes tenuifolia showed highest amount of total phenol content (11.32 ± 0.28 mg/gm GAE) followed by chloroform fraction (9.71 ± 0.31 mg/gm GAE) > N-hexane fraction (6.69 ± 0.67 mg/gm GAE) > ethyl acetate fraction (5.36 ± 0.54 mg/gm GAE). The methanol fraction of Cheilanthes tenuifolia possessed highest amount (7.11 ± 0.52 mg/gm QE) of total flavonoid content. Our present study indicates that methanol extract was most potent (IC 50 = 9.926 μg/ml) inhibitor of DPPH free radicals. In brine shrimp lethality bio assay, all the extracts showed dose dependent increment of mortality and chloroform extract was found most cytotoxic (LC 50 = 34.493 μg/ml) compared to other plant extracts. The chloroform fraction of Cheilanthes tenuifolia was most potent in terms of thrombolytic activity. A compound was isolated (CT-2) using column chromatography followed by TCL and PTLC (35% pet ether in CHCl 3 ) and analyzed by 1 H-NMR. The structure of stigmasterol was confirmed by comparing the 1 H-NMR data with previously published phytochemistry report.Conclusion: Cheilanthes tenuifolia could be a potential candidate for bioactive compounds and further studies on isolation and characterization of its bioactive compounds are highly required.
Background: The significant study was made to investigate the interaction of an antidiabetic drug, glimepiride with bovine serum albumin (BSA) by fluorescence quenching method in two different temperatures (298K and 308K). Methods: The study was carried out through fluorescence spectroscopic analysis. Stern-Volmer equation determined the fluorescence quenching constant. The various thermodynamic parameters such as free energy (ΔG), enthalpy (ΔH), and entropy (ΔS) was found out by Van’t Hoff equation. Results: The data revealed that glimepiride interact with BSA and both tryptophan and tyrosine residues of BSA are responsible for interactions with glimepiride. BSA undergo static quenching in presence of glimepiride, a quencher. The hydrophobic forces participated in chief roles for BSA-glimepiride complexation and this was indicated by the values of thermodynamic parameters. The binding number (n) obtained was ≈1 pointed out that glimepiride and BSA has bound with 1:1 ratio. Conclusions: Through fluorescence spectroscopic technique we revealed the nature of interaction of glimepiride with BSA, quenching mechanism for the interaction and associated thermodynamic parameters.
The study aims to investigate the protein binding kinetics of nicotine and a PPI (pantoprazole) with Bovine Serum Albumin (BSA) through UV spectroscopy and computational modeling. Data was obtained by using nicotine and pantoprazole and warfarin and diazepam as the two site specific probes on Bovine serum albumin (BSA). In-vitro and in-silico modeling was carried out in creating an environment that simulates the body environment. Cellulose membrane tubes were cut into 9 cm and tied tightly not to let any mixtures leak out. To determine number of binding sites, association constants by using Scatchard plot, predominant binding site of each drug and rise in % of free fraction of one by the other were analyzed using equilibrium dialysis method. Molecular docking further verifies the observations. In Scatchard plot analysis, for nicotine, n 1 , n 2 , k 1 and k 2 = 2.2, 7.6, 0.18 µM −1 and 0.02 µM −1 and for pantoprazole, n 1 , n 2 , k 1 and k 2 = 0.42, 1.2, 0.40 µM −1 and 0.03 µM −1. Nicotine binds more to diazepam site (site-II) and pantoprazole mainly to warfarin site (site-I). In molecular docking, the binding affinity of nicotine being −5.7 kcal/mole demonstrates higher affinity for site-II than that of pantoprazole whose binding affinity is −8.0 kcal/mole. In absence and presence of warfarin, the free fraction of pantoprazole bound to BSA (1:1) was increased from 37.79% to 82.44% and 51.78% to 98.80% respectively by nicotine. On the other hand, free fraction of nicotine was raised by pantoprazole from 12.89% to 75.70% and 50.08% to 99.66% in the absence and presence of diazepam. Both the results of spectroscopic and computational molecular docking suggest that administering pantoprazole with nicotine might increase the % free fraction of pantoprazole more. Thus, nicotine consumption can be beneficial for smoker people taking PPI like pantoprazole.
The binding of Ketorolac and Omeprazole to bovine serum albumin (BSA) was studied by equilibrium dialysis method followed by UV spectroscopy. Warfarin and Diazepam were used as site-I and site-II specific probe, respectively. The binding of Ketorolac and Omeprazole was characterized by two sets of association constant: high affinity association constant (K1) with low capacity binding site (n1) and low affinity association constant (K1) with high capacity binding site (n1). In this study, n1 and n1 values were found to be 0.25 ± 0.006 and 1.8 ± 0.025 for Ketorolac and 0.22 ± 0.030 and 1.3±0.035 for Omeprazole at pH 7.4 and 37°C, respectively. At the same condition, the values of K1 and K1 for Ketorolac were found to be 0.624 ± 0.033 ?M-1 and 0.133 ± 0.023 ?M-1 and that of Omeprazole were 0.51 ± 0.001 ?M-1 and 0.28 ± 0.005 ?M-1, respectively. Site specific probe displacement studies implied that both Ketorolac and Omeprazole bind predominantly to site-II, the Diazepam site. In the present study, both Ketorolac and Omeprazole increased the free fraction of each other when they simultaneously bound to BSA. They compete for a common binding site on the albumin molecule, thereby free fraction of both the drugs was increased as compared to the level obtained when the drugs were given individually. We, thus, conclude that during concurrent administration of Ketorolac and Omeprazole adequate precautions should be taken. However, further studies are needed on in-vivo model to substantiate the findings from in-vitro experiments. DOI: http://dx.doi.org/10.3329/bpj.v17i1.22323 Bangladesh Pharmaceutical Journal 17(1): 92-98, 2014
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