Interaction of novel hybrid compounds with the D3 dopamine receptor: Site-directed mutagenesis and homology modeling studies

Biochemical Pharmacology

Volumn 81, Issue 1, 2011, Pages 157-163

  Kortagere, Sandhya ^a   Cheng, Shu Yuan ^b   Antonio, Tamara ^b   Zhen, Juan ^b   Reith, Maarten E A ^b   Dutta, Aloke K ^c  

^a DREXEL UNIVERSITY COLLEGE OF MEDICINE   (United States)

^b NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c WAYNE STATE UNIVERSITY   (United States)

Author keywords

5 OH DPAT; 7 OH DPAT; Dopamine D3 receptor; Homology modeling; Hybrid dopamine agonists; Parkinson's disease

Indexed keywords

2 DIPROPYLAMINO 5 HYDROXYTETRALIN; 2 DIPROPYLAMINO 7 HYDROXYTETRALIN; ASPARTIC ACID; DOPAMINE 3 RECEPTOR; DOPAMINE 3 RECEPTOR STIMULATING AGENT; DOPAMINE RECEPTOR STIMULATING AGENT; RADIOLIGAND; SERINE; SPIPERONE; THREONINE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; BINDING ASSAY; BINDING COMPETITION; BINDING SITE; CELL STRAIN HEK293; CONTROLLED STUDY; HUMAN; HUMAN CELL; HYDROGEN BOND; LIGAND BINDING; MOLECULAR DOCKING; MOLECULAR MODEL; MUTATION; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; RECEPTOR AFFINITY; RECEPTOR BINDING; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; COMPUTER SIMULATION; DOPAMINE AGONISTS; HUMANS; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN CONFORMATION; RECEPTORS, DOPAMINE D3; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 78549284860     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2010.08.026     Document Type: Article

References (32)

1. Emilien G., Maloteaux J.-M., Geurts M., Hoogenberg K., Cragg S. Dopamine receptors-physiological understanding to therapeutic intervention potential. Pharmacol Ther 1999, 84:133-156.
2. Missale C., Nash S.R., Robinson S.W., Jaber M., Caron M.G. Dopamine receptors: from structure to function. Physiol Rev 1998, 78:189-225.
3. D'Ischia M., Prota G. Biosynthesis, structure, and function of neuromelanin and its relation to Parkinson's disease: a critical update. Pigment Cell Res 1997, 10:370-376.
4. Gurevich E.V., Joyce J.N. Distribution of dopamine D3 receptor expressing neurons in the human forebrain: comparison with D2 receptor expressing neurons. Neuropsychopharmacology 1999, 20:60-80.
5. Dutta A.K., Fei X.-S., Reith M.E.A. A novel series of hybrid compounds derived by combining 2-aminotetralin and piperazine fragments: binding activity at D2 and D3 receptors. Bioorg Med Chem Lett 2002, 12:619-622.
6. Dutta A.K., Venkataraman S.K., Fei X.-S., Kolhatkar R., Zhang S., Reith M.E.A. Synthesis and biological characterization of novel hybrid 7-{[2-(4-phenyl-piperazin-1-yl)-ethyl]-propyl-amino}-5,6,7,8-tetrahydro-naphthalen-2-ol and their heterocyclic bioisosteric analogues for dopamine D2 and D3 receptors. Bioorg Med Chem 2004, 12:4361-4373.
7. Biswas S., Zhang S., Fernandez F., Ghosh B., Zhen J., Kuzhikandathil E., et al. Further structure-activity relationships study of hybrid 7-{[2-(4-phenylpiperazin-1-yl)ethyl]propylamino}-5,6,7,8-tetrahydronaphthalen-2-ol analogues: identification of a high-affinity D3-preferring agonist with potent in vivo activity with long duration of action. J Med Chem 2008, 51:101-117.
8. Biswas S., Hazeldine S., Ghosh B., Parrington I., Kuzhikandathil E., Reith M.E., et al. Bioisosteric heterocyclic versions of 7-{[2-(4-phenyl-piperazin-1-yl)ethyl]propylamino}-5,6,7,8-tetrahydronaphth alen-2-ol: identification of highly potent and selective agonists for dopamine D3 receptor with potent in vivo activity. J Med Chem 2008, 51:3005-3019.
9. Brown D.A., Kharkar P.S., Parrington I., Reith M.E., Dutta A.K. Structurally constrained hybrid derivatives containing octahydrobenzo[g or f]quinoline moieties for dopamine D2 and D3 receptors: binding characterization at D2/D3 receptors and elucidation of a pharmacophore model. J Med Chem 2008, 51:7806-7819.
10. Cox B.A., Henningsen R.A., Spanoyannis A., Neve R.L., Neve K.A. Contributions of conserved serine residues to the interactions of ligands with dopamine D2 receptors. J Neurochem 1992, 59:627-635.
11. Sartania N., Strange P.G. Role of conserved serine residues in the interaction of agonists with D3 dopamine receptors. J Neurochem 1999, 72:2621-2624.
12. Lundstrom K., Turpin M.P., Large C., Robertson G., Thomas P., Lewell X.Q. Mapping of dopamine D3 receptor binding site by pharmacological characterization of mutants expressed in CHO cells with the Semliki Forest virus system. J Recept Signal Transduct Res 1998, 18:133-150.
13. Wiens B.L., Nelson C.S., Neve K.A. Contribution of serine residues to constitutive and agonist-induced signaling via the D2S dopamine receptor: evidence for multiple, agonist-specific active conformations. Mol Pharmacol 1998, 54:435-444.
14. Mansour A., Meng F., Meador-Woodruff J.H., Taylor L.P., Civelli O., Akil H. Site-directed mutagenesis of the human dopamine D2 receptor. Eur J Pharmacol 1992, 227:205-214.
15. Varady J., Wu X., Fang X., Min J., Hu Z., Levant B., et al. Molecular modeling of the three-dimensional structure of dopamine 3 (D3) subtype receptor: discovery of novel and potent D3 ligands through a hybrid pharmacophore- and structure-based database searching approach. J Med Chem 2003, 46:4377-4392.
16. Ehrlich K., Gotz A., Bollinger S., Tschammer N., Bettinetti L., Harterich S., et al. Dopamine D2, D3, and D4 selective phenylpiperazines as molecular probes to explore the origins of subtype specific receptor binding. J Med Chem 2009, 52:4923-4935.
17. Zhen J., Antonio T., Dutta A.K., Reith M.E. Concentration of receptor and ligand revisited in a modified receptor binding protocol for high-affinity radioligands: [3H]spiperone binding to D2 and D3 dopamine receptors. J Neurosci Methods 2010, 188:32-38.
18. Cheng Y., Prusoff W.H. Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction. Biochem Pharmacol 1973, 22:3099-3108.
19. Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994, 22:4673-4680.
20. Cherezov V., Rosenbaum D.M., Hanson M.A., Rasmussen S.G., Thian F.S., Kobilka T.S., et al. High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor. Science 2007, 318:1258-1265.
21. Sanchez R., Sali A. Evaluation of comparative protein structure modeling by MODELLER-3. Proteins 1997, Suppl. 1:50-58.
22. Kalé L.S., Bhandarkar R., Brunner M., Gursoy R., Krawetz A., Phillips N., et al. NAMD2: greater scalability for parallel molecular dynamics. J Comput Phys 1999, 151:283-312.
23. Brooks B.R., Bruccoleri R.E., Olafson B.D., States D.J., Swaminathan S., Karplus M. CHARMM: a program for macromolecular energy, minimization, and dynamics calculations. J Comput Chem 1983, 4:187-217.
24. Tama F., Sanejouand Y.H. Conformational change of proteins arising from normal mode calculations. Protein Eng 2001, 14:1-6.
25. Halgren T.A. Merck molecular force field. I. Basis, form, scope, parameterization, and performance of MMFF94. J Comput Chem 1996, 17:490-519.
26. Gasteiger J., Marsili M. Iterative partial equalization of orbital electronegativity-a rapid access to atomic charges. Tetrahedron 1980, 36:3219-3228.
27. Jones G., Willett P., Glen R.C., Leach A.R., Taylor R. Development and validation of a genetic algorithm for flexible docking. J Mol Biol 1997, 267:727-748.
28. Eldridge M.D., Murray C.W., Auton T.R., Paolini G.V., Mee R.P. Empirical scoring functions: I. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes. J Comput Aided Mol Des 1997, 11:425-445.
29. Kortagere S., Welsh W.J. Development and application of hybrid structure based method for efficient screening of ligands binding to G-protein coupled receptors. J Comput Aided Mol Des 2006, 20:789-802.
30. Costanzi S. On the applicability of GPCR homology models to computer-aided drug discovery: a comparison between in silico and crystal structures of the beta2-adrenergic receptor. J Med Chem 2008, 51:2907-2914.
31. Kortagere S., Roy A., Mehler E.L. Ab initio computational modeling of long loops in G-protein coupled receptors. J Comput Aided Mol Des 2006, 20:427-436.
32. Shi L., Javitch J.A. The second extracellular loop of the dopamine D2 receptor lines the binding-site crevice. Proc Natl Acad Sci USA 2004, 101:440-445.