A sensitive LC-MS/MS method has been developed and validated for the quantitative determination of Dexlansoprazole from the commercially available formulations. Omeprazole was used as the internal standard. Isocratic separation was achieved using Zorbax SB C 18 column (4.6 × 100 mm, 3 µm) as a stationary phase and the mobile phase consists of (0.5 mM) Ammonium Acetate adjusted to pH 3.5: acetonitrile (30:70 V/V) with a flow of 0.5 mL/min. Detection was carried out by triple quadrupole mass spectrometry with electrospray ionization in positive mode with proton adducts at m/z 370.05 to 251.95 and 346.00 to 198.05 to monitor Dexlansoprazole and Omeprazole. The linearity of the method was found over a concentration range of 0.5-3000 ng/mL with a regression analysis of 0.9994. The percentage recovery of the present method was found to be 94.33 to 99.97%. The LC-MS/MS method was validated as per ICH guidelines. The developed method can be successfully applied for the estimation of Dexlansoprazole in the commercial formulation and in bulk drug.
Background: CCR5 and/or CXCR4 receptors on CD4+ T cell membranes are the active sites for HIV to bind. The different classes of drugs have unique mechanism of action to cease the virus but we are concentrating in the first class i.e. NNRTI that destroys the virus while it binds to the cell surface gp120 protein. The drugs are having several impurities that can be genotoxic and few are reported in the monographs. Objective: This study proposes the affinity of the impurities to the active site through molecular docking to a receptor (PDB ID 4MBS) from the library of analogues available for the antiretroviral drugs. As these drugs are taken for long term, this study will give a prominent idea for testing the impurities and its genotoxicity. Method: We have done molecular docking of 37 impurities and drugs with GLIDE module of schrodinger software for their binding affinities. In this study, receptor CCR5 and/or CXCR4 is selected containing glycoprotein that mediates virus binding to CD4+ T cell. Results: Didanosine E and Zidovudine D shows maximum and minimum score respectively. The selected impurities were interfering with the active binding site that may lead to any ADR or reduce the effect of API. Conclusion: Conclusively, a significant role is played by Protein-Ligand interaction in structural based designing. Summarizing that there might be genotoxicity effect due to competition between API and the impurities. The molecular docking was used to study the binding mechanism and to establish the docking score along with the activity. The outcome of the study can be used to design and development of novel compounds having genotoxicity.
Papain a proteolytic enzyme is one of the enzymes which have various applications in regard to the food and chemical industry. Papain is isolated by cutting or making incision on the unripe fruit of papaya. Papain enzyme is more active in unripe green fruit. Papaya contains a papain enzyme which will be more helpful in treating the causes of trauma, allergies and sports injuries also papain has a superior digestion action when compare to pepsin and pancreatin. Papain is used variously in textile, pharmaceutics and cosmetics. The papain is extracted from the latex of papaya which is a major chemical compound used in various industries for numerous pharmaceutical and industrial products. Researchers interest towards the enzymes including papain enzyme and it health benefits is favorable. Fusion of papain in various food systems, it has its own stability issues which concerns in deactivate or denature of papain enzyme when it comes in contact with acidic pH inside the body. Several mechanical and chemical processes based on encapsulation techniques have emerged that have been tailored to suit the encapsulation of various food bioactive compounds. Therefore, in order to protect the nature of papain enzyme, Encapsulation/ Formulation has been proposed as an option. After the Encapsulation/ Formulation is done the enzyme will improves its stability issues, maximum therapeutic potential, and also helps in the oral bioavailability and effective oral delivery of the Papain enzyme.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.