Mangalayatan University

About: Mangalayatan University is a education organization based out in Aligarh, Uttar Pradesh, India. It is known for research contribution in the topics: Epitope & Population. The organization has 99 authors who have published 106 publications receiving 1697 citations.

Nanomedicines in Diagnosis and Treatment of Cancer: An Update.

Abstract: Nanomedicine has revolutionized the field of cancer detection and treatment by enabling the delivery of imaging agents and therapeutics into cancer cells. Cancer diagnostic and therapeutic agents can be either encapsulated or conjugated to nanosystems and accessed to the tumor environment through the passive targeting approach (EPR effect) of the designed nanomedicine. It may also actively target the tumor exploiting conjugation of targeting moiety (like antibody, peptides, vitamins, and hormones) to the surface of the nanoparticulate system. Different diagnostic agents (like contrast agents, radionuclide probes and fluorescent dyes) are conjugated with the multifunctional nanoparticulate system to achieve simultaneous cancer detection along with targeted therapy. Nowadays targeted drug delivery, as well as the early cancer diagnosis is a key research area where nanomedicine is playing a crucial role. This review encompasses the significant recent advancements in drug delivery as well as molecular imaging and diagnosis of cancer exploiting polymer-based, lipid-based and inorganic nanoparticulate systems.

Design of novel multi-epitope vaccines against severe acute respiratory syndrome validated through multistage molecular interaction and dynamics

Abstract: Severe acute respiratory syndrome (SARS) is endemic in South China and is continuing to spread worldwide since the 2003 outbreak, affecting human population of 37 countries till present. SARS is ca...

A Fast and Validated Reversed-Phase HPLC Method for Simultaneous Determination of Simvastatin, Atorvastatin, Telmisartan and Irbesartan in Bulk Drugs and Tablet Formulations

Abstract: The aim of this study was to develop and validate a fast and simple reversed-phase HPLC method for simultaneous determination of four cardiovascular agents-atorvastatin, simvastatin, telmisartan and irbesartan in bulk drugs and tablet oral dosage forms. The chromatographic separation was accomplished by using Symmetry C18 column (75 mm × 4.6 mm; 3.5 μ) with a mobile phase consisting of ammonium acetate buffer (10 mM; pH 4.0) and acetonitrile in a ratio 40:60 v/v. Flow rate was maintained at 1 mL/min up to 3.5 min, and then suddenly changed to 2 mL/min till the end of the run (7.5 min). The data was acquired using ultraviolet detector monitored at 220 nm. The method was validated for linearity, precision, accuracy and specificity. The developed method has shown excellent linearity (R² > 0.999) over the concentration range of 1-16 µg/mL. The limits of detection (LODs) and limits of quantification (LOQs) were in the range of 0.189-0.190 and 0.603-0.630 µg/mL, respectively. Inter-day and intra-day accuracy and precision data were recorded in the acceptable limits. The new method has successfully been applied for quantification of all four drugs in their tablet dosage forms with percent recovery within 100 ± 2%.

Allosteric inhibition of aminopeptidase N functions related to tumor growth and virus infection.

Abstract: Cell surface aminopeptidase N (APN) is a membrane-bound ectoenzyme that hydrolyzes proteins and peptides and regulates numerous cell functions. APN participates in tumor cell expansion and motility, and is a target for cancer therapies. Small drugs that bind to the APN active site inhibit catalysis and suppress tumor growth. APN is also a major cell entry receptor for coronavirus, which binds to a region distant from the active site. Three crystal structures that we determined of human and pig APN ectodomains defined the dynamic conformation of the protein. These structures offered snapshots of closed, intermediate and open APN, which represent distinct functional states. Coronavirus envelope proteins specifically recognized the open APN form, prevented ectodomain progression to the closed form and substrate hydrolysis. In addition, drugs that bind the active site inhibited both coronavirus binding to cell surface APN and infection; the drugs probably hindered APN transition to the virus-specific open form. We conclude that allosteric inhibition of APN functions occurs by ligand suppression of ectodomain motions necessary for catalysis and virus cell entry, as validated by locking APN with disulfides. Blocking APN dynamics can thus be a valuable approach to development of drugs that target this ectoenzyme.