Mr. Jagmohan Singh Saini

Gohlke Group Institute of Pharmaceutical and Medicinal Chemistry Heinrich Heine University Universitätsstr.1, Geb. 26.23 O0.22 40225 Düsseldorf, Germany  +49(0)211-81-12528

Mini Academic CV

University degrees:

First degree or intermediate examination:

• Bachelor of Pharmacy, 2003, HNB Garhwal University, SGRRITS, Dehradun, India

Second degree and/or intermediate examination:

• M. S. (PHARM.), 2005, National Institute of Pharmaceutical Education and Research (NIPER), Mohali, Punjab, India

Publications:

• viney Lather, Jagmohan Singh Saini, Rajendra Kristam, Narasingapuram Arumugam Karthikeyan and Vitukudi Narayana Balaji; “QSAR Models for Prediction of Glycogen Synthase Kinase-3b Inhibitory Activity of Indirubin Derivatives”, QSAR and Combinatorial Science, Volume 27, Issue 6, June 2008, Pages: 718-728
• Jagmohan S Saini; “Informatics in pharmaceutical sciences”, Express Pharma Pulse (Dec, 2004) [contribution in In Silico ADME/Tox]

Attended conferences:

• International Conference on Open Source For Computer Aided Drug Discovery held at IMTECH (March, 2009), India.
• Workshop on Molecular Modeling and Pharmacoinformatics held at NIPER (March, 2008), India.
• Fourth Indo-US workshop in Mathematical Chemistry with application to Drug Discovery, Environmental toxicology, Chemoinformatics & Bioinformatics, at Pune, Maharashtra (January, 2005), India
• National Symposium on Medicine Information held in NIPER (August, 2003), India

BioStruct PhD project

Determinants of selectivity, action, and resistance of antibiotics binding to prokaryotic and eukaryotic ribosomes
Several classes of antibiotics specifically inhibit the activity of ribosomes by binding to the peptidyl transferase center (PTC) and the ribosomal exit tunnel region at adjacent or overlapping sites. Available high-resolution structures of antibiotics bound to ribosomal subunits provide crucial insights regarding the binding sites, binding modes, and mechanism of action for several antibiotics. This information creates possibilities to suggest chemical modifications to achieve higher binding affinity and selectivity of antibiotics or even new classes of anti-bacterial drugs. However, the structure elucidation only provides a static view of the binding processes, but does neither reveal the dynamics governing ribosomal function nor the energetic determinants of antibiotics binding. Molecular dynamics simulations (MD) in combination with free energy calculations are suitable to fill this gap. So far, neither the PTC nor the ribosomal exit tunnel have been investigated in complex with bound antibiotics by these techniques. The goal of this project is to investigate for the first time dynamical and energetic properties of antibiotic-ribosome complexes in atomic detail by MD in combination with free energy calculations. This provides a unique opportunity for a detailed analysis of antibiotics selectivity, action, and resistance in terms of energetics of binding, influences of structural components of more extended binding site regions, and resistance mechanisms resembling allosteric effects.


Topic Supervisor: Prof. Dr. Holger Gohlke, Institute of Pharmaceutical and Medicinal Chemistry, Heinrich Heine University Duesseldorf, Gohlke Group

Complementary Supervisor: Prof. Dr. Gerhard Steger

BioStruct Fellow: Mr. Jagmohan Singh Saini

Contact

NRW Research School BioStruct

Chairmen:
Prof. Dr. Lutz Schmitt


Prof. Dr. Dieter Willbold


Managing Director:
Dr. Christian Dumpitak


Scientific Coordinator:
Dr. Cordula Kruse



c/o
Institut für Physikalische Biologie
Heinrich-Heine-Universität Düsseldorf
Geb. 26.12.U1
Universitätsstr. 1
40225 Düsseldorf
Germany

+49-211-81-15314/14826
+49-211-81-15167