Irshad Ahmad

Irshad Ahmad
Indian Institute of Technology Delhi | IIT Delhi · Department of Chemistry

Ph. D. Biosciences

About

11
Publications
13,309
Reads
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64
Citations
Citations since 2017
9 Research Items
62 Citations
2017201820192020202120222023051015
2017201820192020202120222023051015
2017201820192020202120222023051015
2017201820192020202120222023051015
Introduction
I am Dr. Irshad Ahmad, have completed my doctoral studies at the Department of Biosciences, Jamia Millia Islamia ( A Central University) in New Delhi, Presently I am working as a young scientist at the Indian Institute of Technology Delhi. My research interests include understanding the molecular and biochemical basis of thrombosis and Hemostasis and understanding their mechanistic aspect to develop therapeutics.
Additional affiliations
March 2018 - March 2021
Jamia Millia Islamia
Position
  • Senior Researcher
September 2013 - August 2019
Jamia Millia Islamia
Position
  • PhD Student

Publications

Publications (11)
Article
Thromboembolic diseases are a major cause of mortality in human and the currently available anticoagulants are associated with various drawbacks, therefore the search for anticoagulants that have better safety profile is highly desirable. Compounds that are part of the dietary routine can be modified to possibly increase their anticoagulant potenti...
Article
Full-text available
Aims Design and synthesis of a novel 3, 3', 4', 5, 7-O- pentasulfated Quercetin (QPS) as activator of protein disulfide isomerase (PDI). Main Methods Based on an in silico analysis we show that QPS binds to a and b domain of PDI (-7.4 kcal/mol) unlike PDI inhibitor quercetin 3-rutinoside (Q3R) that binds at substrate binding domain b (-8.0 kcal/mo...
Article
Full-text available
Serine protease inhibitors (serpins) family have a complex mechanism of inhibition that requires a large scale conformational change. Antithrombin (AT), a member of serpin superfamily serves as a key regulator of the blood coagulation cascade, deficiency of which leads to thrombosis. In recent years, a handful of studies have identified small compo...
Article
Currently available anticoagulants for prevention and treatment of thrombosis have several limitations, thus, small organic scaffolds that can dissolve clots in vivo in a dose dependent manner with lesser side effects are highly desirable. Here we report the synthesis of esculin pentasulfate (EPS) and assessment of its in vitro, in vivo and ex vivo...
Article
Pro-coagulant, anti-coagulant and fibrinolytic pathways are responsible for maintaining haemostatic balance under physiological conditions. Any deviation from these pathways would result in hypercoagulability leading to life threatening diseases like myocardial infarction, stroke, portal vein thrombosis, deep vein thrombosis (DVT) and pulmonary emb...

Questions

Questions (9)
Question
What is the safest anticoagulant used presently with the least side effects?
Question
As we all are aware in the recent two decades, many new anti-thrombotic drugs have been designed, still they require regular monitoring and have reasonable drawbacks.
I would like to know about new strategies and possible mechanisms to be targeted for conducting anti-thrombotic studies.
Question
The synthesis of sulfated compounds is intricate to achieve and percentage yield of the product is low. The reaction leads to formation of many conjugates thereby making it difficult to isolate sulfated compound from the reaction mixture. Moreover most of sulfated compounds are water soluble compounds, therefore to purify these compounds becomes very difficult. What are the different ways to purify sulfated compounds other then RP-HPLC?
Question
I purify antithrombin using Hi trap heparin prepacked column. After five to six purification's the column gets yellowish and remains the same even after extensive washing. The binding of protein also gets hampered. Kindly suggest any method that can help to clean the column properly.
Question
I Have purified my protein with Ni NTA chromatography.In second step chromatography i have used anion exchange chromatography to remove dimer from monomer.my protein PI is 4.9.i have no problem so far.i got single band at 45 kd with respect of my protein after anion exchange chromatography.(no dimer at all,please see the attachment)
My protein elute at ~300 mM Nacl and 30 mM bis tris.2% glycerol.pH-7(AEC)and i stored my protein at -80.
my questions are
1. Is high salt concn cause problem during protein storage?
2.that dimer came back (very less as observed in sds)how can i prevent that dimer formation later during my experiment.(i used protein after thawing)
how can i overcome all these problem.we have no akta system.i did it manually.please give me suggestions.
My protein elute at ~300 mM Nacl and 30 mM bis tris.2% glycerol.pH-7(AEC)and i stored my protein at -80.
my questions are
1. Is high salt concn cause problem during protein storage?
2.that dimer came back (very less as observed in sds)how can i prevent that dimer formation later during my experiment.(i used protein after thawing)
how can i overcome all these problem.we have no akta system.i did it manually.please give me suggestions.
Question
There is only about 20-50 mgs of product and i need all DMA must be removed as it will effect to my studies. so all i really need to do is remove the DMA.
are there any co-solvents one can add to help with the lyophilization? 
is there something else that i can do to remove the DMA?
any suggestions would be appreciated.
Question
What is the best possible way to remove Dimethylacetamide (DMA) from reaction mixture ? Through rota evaporator and vacuum pump i couldn't remove DMA.
Kindly enlighten me regarding this.
Question
How to calculate dosage for in vivo  from in vitro data ?

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Projects

Projects (3)
Project
To study molecular dynamics of novel, effective anticoagulants.
Project
To study novel, effective anti-thrombotic agent.