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Dr Irina Tikhonova

General Profile Information
Staff Name Dr Irina Tikhonova
Job Title Lecturer
Location Pharmacy & MCI Block 98 MBC Site
Room Number 02.061
School School of Pharmacy
Contact Details
Telephone +44 (0)28 9097 2202


       Medicinal computational chemistry, computational biology, chemoinformatics,

       structural bioinformatics and pharmacology of G protein-coupled receptors.



   PMY2002: Medicinal Substances: Structure and Function

   PMY3082: Drug Design and Applied Pharmaceutical Analysis

   BBC3034: Biomolecular Structure

   PMY4005: Research Project

   PMY1014: Introduction to Communicational Skills 


  Irina Tikhonova pursued a Ph.D. in molecular modelling of the ionotropic glutamate receptors at the Moscow State University,  Russia. In 2004, after her PhD, she became a postdoctoral fellow at the Institute of Molecular Medicine, Toulouse, France,        where she studied ligand-protein interactions in the G protein coupled receptors (GPCRs), on the example of the    cholecystokinin and gastrin receptors, using molecular docking and, tested her modeling hypotheses collaborating with        experimental biologists. In 2005 she continued structure-function relationship investigations of GPCRs and conducted      knowledge-based drug design of the free fatty acid receptor ligands, applying bio/chemoinformatics methods, virtual screening  and molecular dynamics and, working in the multidisciplinary team that included pharmacologists, medicinal chemists and    physicists at the National Institutes of Health near Washington DC, USA.  In 2009 she joined Queen's as a Lecturer in    Molecular Modelling.

Research Statement


 Our general research activities focus on improving and applying computational methods to integrate chemistry, biology and  medicine of drug targets. The current activities focus on molecular docking and simulations of the G protein-coupled receptors  (GPCRs). Using experimental results obtained through collaborations along with internet systems chemical biology  resources; we apply different molecular modelling methods to develop new approaches for the design of novel small molecule  ligands for GPCRs and enzymes.

    Currently Active Programs:

  - Study of protease flexibility on the example of prostasin using a multi-scale simulation approach. 

   (In collaboration with Prof. Brain Walker)

  -Understanding organization, dynamics and interactions of the bioamine receptors using molecular dynamics

    studies in realistic environment.

  - Identification of orthosteric and allsteric binding sites in the free fatty acid receptors (FFA2-3).

   (In collaboration with Prof. Graeme Milligan, University of Glasgow)

  - Structure-based design of peptide mimetics for the gastric inhibitory polypeptide (GIP)

  (In collaboration with Prof. Fourmy, Toulouse University)

Professional Qualifications

I regularly review grant applications for the UK Research Councils (EPSRC, BBSRC and MRC)


I regularly review manuscripts for ACS Journal of Medicinal Chemistry,  Journal of American Chemical Society, Future Medicinal Chemistry, Organic Biomolecular Chemistry, Proteins: Structure, Function and Bioinformatics, Current Physical Chemistry, Journal of Pharmacy and Pharmacology). 

Membership Of Other Societies / Professional Activities


Awards And Honours/major Prizes



Other Information

TitleJournal NameYear
Comparison of Dynamics of Extracellular Accesses to the β(1) and β(2) Adrenoceptors Binding Sites Uncovers the Potential of Kinetic Basis of Antagonist Selectivity. Chemical Biology & Drug Design Vol 10  DOI 2012
Probing the mid-gorge of cholinesterases with spacer-modified bivalent quinazolinimines leads to highly potent and selective butyrylcholinesterase inhibitors. Bioorganic & Medicinal Chemistry Vol 19(3) (1222-1235)  DOI   2011
Selective orthosteric free fatty acid receptor 2 (FFA2) agonists: identification of the structural and chemical requirements for selective activation of FFA2 versus FFA3. The Journal of biological chemistry Vol 286 (1222-1235)  DOI   2011
Extracellular loop 2 of the free Fatty Acid receptor 2 mediates allosterism of a phenylacetamide ago-allosteric modulator. Molecular Pharmacology Vol 80(1) (163-173)  DOI   2011
The family of G protein-coupled receptors: an example of membrane proteins. Methods in molecular biology (Clifton, N.J.) Vol 654 (441-454)  DOI 2010
Identification of determinants of glucose-dependent insulinotropic polypeptide receptor that interact with N-terminal biologically active region of the natural ligand. Molecular Pharmacology Vol 77(4) (547-558)  DOI 2010
Unraveling the structure and function of G protein-coupled receptors through NMR spectroscopy. Current pharmaceutical design Vol 15(35) (4003-4016)  2009
Rhodopsin and the others: a historical perspective on structural studies of G protein-coupled receptors. Current pharmaceutical design Vol 15(35) (3994-4002)  2009
Two arginine-glutamate ionic locks near the extracellular surface of FFAR1 gate receptor activation. The Journal of biological chemistry Vol 284(6) (3529-3536)  DOI 2009
Evidence for a direct and functional interaction between the regulators of G protein signaling-2 and phosphorylated C terminus of cholecystokinin-2 receptor. Molecular Pharmacology Vol 75(3) (502-513)  DOI 2009
Ligand and structure-based methodologies for the prediction of the activity of G protein-coupled receptor ligands. Journal of Computer-Aided Molecular Design Vol 23(11) (747-754)  DOI 2009
Atomistic insights into rhodopsin activation from a dynamic model. Journal of the American Chemical Society Vol 130(31) (10141-10149)  DOI 2008
Discovery of novel agonists and antagonists of the free fatty acid receptor 1 (FFAR1) using virtual screening. Journal of Medicinal Chemistry Vol 51(3) (625-633)  DOI 2008
Insights into the binding and activation sites of the receptors for cholecystokinin and gastrin. Regulatory Peptides Vol 145(1-3) (17-23)  DOI 2008
Identification of residues important for agonist recognition and activation in GPR40. The Journal of biological chemistry Vol 282(40) (29248-29255)  DOI 2007
Mechanism of activation of a G protein-coupled receptor, the human cholecystokinin-2 receptor. The Journal of biological chemistry Vol 282(39) (28779-28790)  DOI 2007
Validated ligand binding sites in CCK receptors. next step: computer-aided design of novel CCK ligands. Current Topics In Medicinal Chemistry Vol 7(12) (1243-1247)  2007
P2Y1 antagonists: combining receptor-based modeling and QSAR for a quantitative prediction of the biological activity based on consensus scoring. Journal of Medicinal Chemistry Vol 50(14) (3229-3241)  DOI 2007
Bidirectional, iterative approach to the structural delineation of the functional Journal of Medicinal Chemistry Vol 50(13) (2981-2989)  DOI 2007
Structure and function of G protein-coupled receptors studied using sequence analysis, molecular modeling and receptor engineering: adenosine receptor. Frontiers in Drug Design and Discovery Vol 3 (63-79)  2007
Target-structure based design and refinement of cholecystokinin and gastrin receptor ligands. Book of Gene and Medicine Vol 8 (73-79)  2007
Modeled structure of the whole regulator G-protein signaling-2. Biochemical and Biophysical Research Communications Vol 341(3) (715-720)  DOI 2006
Partial agonism, neutral antagonism, and inverse agonism at the human wild-type and constitutively active cholecystokinin-2 receptors. Molecular Pharmacology Vol 69(3) (680-690)  DOI 2006
A new mechanism of G protein coupled receptor regulation through direct interaction between RGS2 and phosphorylated C-terminus of cholecystokinin receptor Regulatory Peptides Vol 135 (140-140)  2006
Linking non-peptide ligand binding to partial agonism and inverse agonism at CCK2 receptor Regulatory Peptides Vol 135 (193-193)  2006
Evidence that interspecies polymorphism in the human and rat cholecystokinin receptor-2 affects structure of the binding site for the endogenous agonist cholecystokinin. The Journal of biological chemistry Vol 280(23) (22198-22204)  DOI 2005
Modeled structure of a G-protein-coupled receptor: the cholecystokinin-1 receptor. Journal of Medicinal Chemistry Vol 48(1) (180-191)  DOI 2005
Selectivity fields: comparative molecular field analysis (CoMFA) of the glycine/NMDA and AMPA receptors. Journal of Medicinal Chemistry Vol 46(19) (4063-4069)  DOI 2003
CoMFA and homology-based models of the glycine binding site of N-methyl-d-aspartate receptor. Journal of Medicinal Chemistry Vol 46(9) (1609-1616)  DOI 2003
Structural basis for understanding structure-activity relationships for the glutamate binding site of the NMDA receptor. Journal of Medicinal Chemistry Vol 45(18) (3836-3843)  2002
Reaction of 2,2,3,3-tetracyanocyclopropyl ketons with ammonia. Mendeleev Communication Vol 1 (25-26)  2000
A new route to 1-substituted 2,2,3,3-tetracyanocyclopropanes Russian Journal of General Chemistry Vol 70 (1251-1253)    2000
Reaction of tetracyanoethylene with alpha,beta-unsaturated ketones Russian Journal of Organic Chemistry Vol 36 (593-594)    2000