Synthesis, pharmacological evaluation and conformational investigation of endomorphin-2 hybrid analogues

Molecular Diversity

Volumn 17, Issue 1, 2013, Pages 19-31

  Lesma, Giordano ^a   Salvadori, Severo ^b   Airaghi, Francesco ^a   Bojnik, Engin ^c   Borsodi, Anna ^c   Recca, Teresa ^a   Sacchetti, Alessandro ^d   Balboni, Gianfranco ^e   Silvani, Alessandra ^a  

^a UNIVERSITY OF MILAN   (Italy)

^b UNIVERSITY OF FERRARA   (Italy)

^c INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

^d POLITECNICO DI MILANO   (Italy)

^e UNIVERSITY OF CAGLIARI   (Italy)

Author keywords

Beta amino acid; Endomorphin 2; Molecular docking; Molecular modelling; Opioid receptor; Peptidomimetic

Indexed keywords

ENDOMORPHIN 2; MU OPIATE RECEPTOR;

ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; DRUG SCREENING; DRUG SYNTHESIS; LIGAND BINDING; MOLECULAR DOCKING; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE; RAT; STRUCTURE ACTIVITY RELATION;

AMINO ACIDS; MODELS, MOLECULAR; MOLECULAR CONFORMATION; MOLECULAR DOCKING SIMULATION; MOLECULAR MIMICRY; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OLIGOPEPTIDES; RECEPTORS, OPIOID; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84873413986     PISSN: 13811991     EISSN: 1573501X     Source Type: Journal    
DOI: 10.1007/s11030-012-9399-5     Document Type: Article

References (57)

1. Seebach D, Gardiner J (2008) β-Peptidic peptidomimetics. Acc Chem Res 41: 1366-1375. doi: 10.1021/ar700263g
2. Wu YD, Han W, Wang DP, Gao Y, Zhao YL (2008) Theoretical analysis of secondary structures of β-peptides. Acc Chem Res 41: 1418-1427. doi: 10.1021/ar800070b
3. Cheng RP, Gellman SH, DeGrado WF (2001) β-Peptides: from structure to function. Chem Rev 101: 3219-3232. doi: 10.1021/cr000045i
4. Horne WS, Gellman SH (2008) Foldamers with heterogeneous backbones. Acc Chem Res 41: 1399-1408. doi: 10.1021/ar800009n
5. Vasudev PG, Chatterjee S, Shamala N, Balaram P (2011) Structural chemistry of peptides containing backbone expanded amino acid residues: conformational features of β, γ, and hybrid peptides. Chem Rev 111: 657-687. doi: 10.1021/cr100100x
6. Sacchetti A, Silvani A, Lesma G, Pilati T (2011) Phe-Ala-based diazaspirocyclic lactam as nucleator of type II′ β-turn. J Org Chem 76: 833-839. doi: 10.1021/jo1019927
7. Lesma G, Landoni N, Pilati T, Sacchetti A, Silvani A (2009) Tetrahydroisoquinoline-based spirocyclic lactam as a type II′ β-turn inducing peptide mimetic. J Org Chem 74: 8098-8105. doi: 10.1021/jo901480d
8. Lesma G, Landoni N, Sacchetti A, Silvani A (2007) Pyrroloisoquinoline- based tetrapeptide analogues mimicking reverse-turn secondary structures. J Org Chem 72: 9765-9768. doi: 10.1021/jo701581j
9. Lesma G, Landoni N, Sacchetti A, Silvani A (2010) The spiropiperidine-3,3′-oxindole scaffold: a type II β-turn peptide isostere. Tetrahedron 66: 4474-4478. doi: 10.1016/j.tet.2010.04.077
10. Urman S, Gaus K, Yang Y, Strijowski U, Sewald N, De Pol S, Reiser O (2007) The constrained amino acid β-Acc confers potency and selectivity to integrin ligands. Angew Chem Int Edn 46: 3976-3978. doi: 10.1002/anie.200605248
11. Tyndall JDA, Pfeiffer B, Abbenante G, Fairlie DP (2005) Over one hundred peptide-activated G protein-coupled receptors recognize ligands with turn structure. Chem Rev 105: 793-826. doi: 10.1021/cr040689g
12. Blakeney JS, Reid RC, Le GT, Fairlie DP (2007) Nonpeptidic ligands for peptide-activated G protein-coupled receptors. Chem Rev 107: 2960-3041. doi: 10.1021/cr050984g
13. Horvath G (2000) Endomorphin-1 and endomorphin-2: phar-macology of the selective endogenous μ-opioid receptor agonists. Pharmacol Therapeutics 88:437-463. doi: 10.1016/S0163-7258(00)00100-5
14. Zadina JE, Hackler L, Ge LJ, Kastin AJ (1997) A potent and selective endogenous agonist for the μ-opiate receptor. Nature 386: 499-502. doi: 10.1038/386499a0
15. Fichna J, Janecka A, Costentin J, Do Rego JC (2007) The endomorphin system and its evolving neurophysiological role. Pharmacol Rev 59: 88-123. doi: 10.1124/pr.59.1.3
16. Janecka A, Staniszewska R, Fichna J (2007) Endomorphin Analogs. Curr Med Chem 14: 3201-3208
17. Leitgeb B (2007) Structural investigation of endomorphins by experimental and theoretical methods: hunting for the bioactive conformation. Chem Biodivers 4: 2703-2724. doi: 10.1002/cbdv.200790221
18. Eguchi M (2004) Recent advances in selective opioid receptor agonists and antagonists. Med Res Rev 24: 182-212. doi: 10.1002/med.10059
19. Gentilucci L, Tolomelli A (2004) Recent advances in the investigation of the bioactive conformation of peptides active at the micro-opioid receptor. conformational analysis of endomorphins. Curr Top Med Chem 4: 105-121
20. Gentilucci L, Tolomelli A, De Marco R, Spampinato S, Bedini A, Artali R (2011) The inverse type II β-turn on d-Trp-Phe, a pharmacophoric motif for MOR agonists. ChemMedChem 6: 1640-1653. doi: 10.1002/cmdc.201100169
21. Torino D, Mollica A, Pinnen F, Feliciani F, Lucente G, Fabrizi G, Portalone G, Davis P, Lai J, Ma SW, Porreca F, Hruby VJ (2010) Synthesis and evaluation of new endomorphin-2 analogues containing (Z)-α,β- didehydrophenylalanine (ΔZPhe) Residues. J Med Chem 53: 4550-4554. doi: 10.1021/jm1001343
22. Perlikowska R, Gach K, Fichna J, Tóth G, Walkowiak B, do-Rego JC, Janecka A (2009) Biological activity of endomorphin and [Dmt1]endomorphin analogs with six-membered proline surrogates in position 2. Bioorg Med Chem 17: 3789-3794. doi: 10.1016/j.bmc.2009.04.046
23. Ballet S, Feytens D, De Wachter R, De Vlaemink M, Marczak ED, Salvadori S, de Graaf C, Rognan D, Negri L, Lattanzi R, Lazarus LH, Tourwé D, Balboni G (2009) Conformationally constrained opioid ligands: The Dmt-Aba and Dmt-Aia versus Dmt-Tic scaffold. Bioorg Med Chem Lett 19: 433-437. doi: 10.1016/j.bmcl.2008.11.051
24. Balboni G, Fiorini S, Baldisserotto A, Trapella C, Sasaki Y, Ambo A, Marczak ED, Lazarus LH, Salvadori S (2008) Further studies on lead compounds containing the opioid pharmacophore Dmt-Tic. J Med Chem 51: 5109-5117. doi: 10.1021/jm800587e
25. Tömböly C, Ballet S, Feytens D, Kövér KE, Borics A, Lovas S, Al-Khrasani M, Fürst Z, Tóth G, Benyhe S, Tourwé D (2008) Endomorphin-2 with a β-turn backbone constraint retains the potent μ-opioid receptor agonist properties. J Med Chem 51: 173-177. doi: 10.1021/jm7010222
26. Ballet S, Salvadori S, Trapella C, Bryant SD, Jinsmaa Y, Lazarus LH, Negri L, Giannini E, Lattanzi R, Tourwé D, Balboni G (2006) New 2′,6′-Dimethyl-l-tyrosine (Dmt) opioid peptidomimetics based on the Aba-Gly Scaffold. Development of unique μ-opioid receptor ligands. J Med Chem 49: 3990-3993. doi: 10.1021/jm0603264
27. Tömböly C, Kövér KE, Péter A, Tourwé D, Biyashev D, Benyhe S, Borsodi A, Al-khrasani M, Ronay AZ, Tóth G (2004) Structure-activity study on the phe side chain arrangement of endomorphins using conformationally constrained analogues. J Med Chem 47: 735-743. doi: 10.1021/jm0310028
28. Shao X, Gao Y, Zhu C, Liu X, Yao J, Cui Y, Wang R (2007) Conformational analysis of endomorphin-2 analogs with phenylalanine mimics by NMR and molecular modeling. Bioorg Med Chem 15: 3539-3547. doi: 10.1016/j.bmc.2007.02.050
29. Leitgeb B, Otvos F, Toth G (2003) Conformational analysis of endomorphin-2 by molecular dynamics methods. Biopolymers 68: 497-511
30. Leitgeb B, Szekeres A, Tóth G (2003) Conformational analysis of endomorphin-1 by molecular dynamics methods. Biopolymers. doi: 10.1034/j.1
31. Yu Y, Shao X, Cui Y, Liu H, Wang C, Fan Y, Liu J, Dong S, Cui Y, Wang R (2007) Structure-activity study on the spatial arrangement of the third aromatic ring of endomorphins 1 and 2 using an atypical constrained C terminus. ChemMedChem 2: 309-317. doi: 10.1002/cmdc.200600274
32. Borics A, Tóth G (2010) Structural comparison of μ-opioid receptor selective peptides confirmed four parameters of bioactivity. J Mol Graph Model 28: 495-505. doi: 10.1016/j.jmgm.2009.11.006
33. Caputo R, Cassano E, Longobardo L, Palumbo G (1995) Synthesis of enantiopure N- and C-protected homo-β-amino acids by direct homologation of α-amino acids. Tetrahedron 51: 12337-12350. doi: 10.1016/0040-4020(95) 00778-7
34. Lee HS, Park JS, Kim BM, Gellman SH (2003) Efficient synthesis of enantiomerically pure β2-amino acids via chiral isoxazolidinones. J Org Chem 68: 1575-1578. doi: 10.1021/jo026738b
35. Tessier A, Lahmar N, Pytkowicz J, Brigaud T (2008) Highly diastereoselective synthetic route to enantiopure β2-amino acids and γ-amino alcohols using a fluorinated oxazolidine (Fox) as chiral auxiliary. J Org Chem 73: 3970-3973. doi: 10.1021/jo800562x
36. Albrizio S, Carotenuto A, Fattorusso C, Moroder L, Picone D, Temussi PA, D'Ursi A (2002) Environmental mimic of receptor interaction: conformational analysis of CCK-15 in solution. J Med Chem 45: 762-769. doi: 10.1021/jm0109457
37. Shao X, Gao Y, Zhu C, Liu X, Yao J, Cui Y, Wang R (2007) Conformational analysis of endomorphin-2 analogs with phenylalanine mimics by NMR and molecular modeling. Bioorg Med Chem 15: 3539-3547. doi: 10.1016/j.bmc.2007.02.050
38. Grathwohl C, Wüthrich K (1981) NMR studies of the rates of proline cis-trans isomerization in oligopeptides. Biopolymers 20: 2623-2633. doi: 10.1002/bip.1981.360201209
39. Keresztes A, Szucs M, Borics A, Kövér KE, Forró E, Fülöp F, Tömböly C, Péter A, Páhi A, Fábián G, Murányi M, Tóth G (2008) New endomorphin analogues containing alicyclic β-amino acids: influence on bioactive conformation and pharmacological profile. J Med Chem 51: 4270-4279. doi: 10.1021/jm800223t
40. Mallareddy JR, Borics A, Keresztes A, Kövér KE, Tourwé D, Tóth G (2011) Design, synthesis, pharmacological evaluation, and structure-activity study of novel endomorphin analogues with multiple structural modifications. J Med Chem 54: 1462-1472. doi: 10.1021/jm101515v
41. 3-h-amino acids. J Pept Sci 15: 777- 782
42. Manglik A, Kruse AC, Kobilka TS, Thian FS, Mathiesen JM, Sunahara RK, Pardo L, Weis WI, Kobilka BK, Granier S (2012) Crystal structure of the μ-opioid receptor bound to a morphinan antagonist. Nature 485: 321-326. doi: 10.1038/nature10954
43. Granier S, Manglik A, Kruse AC, Kobilka TS, Thian FS, Weis WI, Kobilka BK (2012) Structure of the δ-opioid receptor bound to naltrindole. Nature 485: 400-404. doi: 10.1038/nature11111
44. Mosberg HI, Fowler CB (2002) Development and validation of opioid ligand-receptor interaction models: the structural basis of μ vs δ selectivity. J Pept Res 60: 329-335
45. Gentilucci L, Tolomelli A, De Marco R, Artali R (2012) Molecular docking of opiates and opioid peptides, a tool for the design of selective agonists and antagonists, and for the investigation of atypical ligand-receptor interactions. Curr Med Chem 19: 1587-1601. doi: 10.2174/092986712799945030
46. Liu X, Kai M, Jin L, Wang R (2009) Molecular modeling studies to predict the possible binding modes of endomorphin analogs in μ opioid receptor. Bioorg Med Chem Lett. doi: 10.1016/j.bmcl.2009.07.121
47. Liu X, Kai M, Jin L, Wang R (2009) Computational study of the heterodimerization between μ and δ receptors. J Computer-Aid Mol Des 23: 321-332. doi: 10.1007/s10822-009-9262-7
48. Urban JD, Clarke WP, Von Zastrow M, Nichols DE, Kobilka B, Weinstein H, Javitch JA, Roth BL, Christopoulos A, Sexton PM, Miller KJ, Spedding M, Mailman RB (2007) Functional selectivity and classical concepts of quantitative pharmacology. J Pharmacol Exp Ther 320: 1-13. doi: 10.1124/jpet.106.104463
49. Nevin ST, Kabasakal L, Otvös F, Tóth G, Borsodi A (1994) Binding characteristics of the novel highly selective delta agonist, [3H]Ile5,6deltorphin II. Neuropeptides 26: 261-265. doi: 10.1016/0143-4179(94) 90080-9
50. Tóth G, Ioja E, Tömböly C, Ballet S, Tourwé D, Péter A, Martinek T, Chung NN, Schiller PW, Benyhe S, Borsodi A (2006) β-Methyl substitution of cyclohexylalanine in dmt-tic-cha-phe peptides results in highly potent δ opioid antagonists. J Med Chem 50: 328-333. doi: 10.1021/jm060721u
51. Spartan '08, Wavefunction, Inc. Irvine, CA
52. Maestro, version 9.0 (2011) Schrödinger, LLC, New York
53. Glide, version 5.5 (2011) Schrödinger, LLC, New York
54. Park M, Gao C, Stern HA (2011) Estimating binding affinities by docking/scoring methods using variable protonation states. Proteins 79: 304-314
55. Friesner RA, Murphy RB, Repasky MP, Frye LL, Greenwood JR, Halgren TA, Sanschagrin PC, Mainz DT (2006) Extra precision glide: docking and scoring incorporating a model of hydrophobic enclosure for protein-ligand complexes. J Med Chem 49: 6177-6196. doi: 10.1021/jm051256o
56. Friesner RA, Banks JL, Murphy RB, Halgren TA, Klicic JJ, Mainz DT, Repasky MP, Knoll EH, Shaw DE, Shelley M, Perry JK, Francis P, Shenkin PS (2004) Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy. J Med Chem 47: 1739-1749. doi: 10.1021/jm0306430
57. Halgren TA, Murphy RB, Friesner RA, Beard HS, Frye LL, Pollard WT, Banks JL (2004) Glide: a new approach for rapid, accurate docking and scoring. 2. enrichment factors in database screening. J Med Chem 47: 1750-1759. doi: 10.1021/jm030644s