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Volumn 4 DEC, Issue , 2013, Pages

Lipid- and sugar-modified endomorphins: Novel targets for the treatment of neuropathic pain

Author keywords

Blood brain barrier; Endomorphin; Glycopeptide; Glycosylation; Lipoamino acid; Lipopeptide; Neuropathic pain; Peptide delivery

Indexed keywords

AMINO ACID; CARBOHYDRATE; DELTORPHIN; ENDOMORPHIN 1; ENDORPHIN; FATTY ACID; GLYCOPEPTIDE; LACTOSE; LEUCINE ENKEPHALIN; LIPOAMINO ACID; METENKEPHALIN; MORPHINE; SUBSTANCE P; UNCLASSIFIED DRUG;

EID: 84891685294     PISSN: None     EISSN: 16639812     Source Type: Journal    
DOI: 10.3389/fphar.2013.00155     Document Type: Review
Times cited : (39)

References (68)
  • 1
    • 0027310350 scopus 로고
    • SDZ CO 611: a highly potent glycated analog of somatostatin with improved oral activity
    • doi: 10.1016/0024-3205(93)90703-6
    • Albert, R., Marbach, P., Bauer, W., Briner, U., Fricker, G., Bruns, C., et al. (1993). SDZ CO 611: a highly potent glycated analog of somatostatin with improved oral activity. Life Sci. 53, 517-525. doi: 10.1016/0024-3205(93)90703-6.
    • (1993) Life Sci. , vol.53 , pp. 517-525
    • Albert, R.1    Marbach, P.2    Bauer, W.3    Briner, U.4    Fricker, G.5    Bruns, C.6
  • 2
    • 0033820226 scopus 로고    scopus 로고
    • Lipophilicity in trans-bilayer transport and subcellular pharmacokinetics
    • doi: 10.1023/A:1008775707749
    • Balaz, S. (2000). Lipophilicity in trans-bilayer transport and subcellular pharmacokinetics. Perspect. Drug Discov. 19, 157-177. doi: 10.1023/A:1008775707749.
    • (2000) Perspect. Drug Discov. , vol.19 , pp. 157-177
    • Balaz, S.1
  • 3
    • 0027055922 scopus 로고
    • Permeability of the blood-brain barrier to peptides: an approach to the development of therapeutically useful analogs
    • doi: 10.1016/0196-9781(92)90037-4
    • Banks, W. A., Audus, K. L., and Davis, T. P. (1992). Permeability of the blood-brain barrier to peptides: an approach to the development of therapeutically useful analogs. Peptides 13, 1289-1294. doi: 10.1016/0196-9781(92)90037-4.
    • (1992) Peptides , vol.13 , pp. 1289-1294
    • Banks, W.A.1    Audus, K.L.2    Davis, T.P.3
  • 4
    • 0022349214 scopus 로고
    • Peptides and the blood-brain barrier: lipophilicity as a predictor of permeability
    • doi: 10.1016/0361-9230(85)90153-4
    • Banks, W. A., and Kastin, A. J. (1985). Peptides and the blood-brain barrier: lipophilicity as a predictor of permeability. Brain Res. Bull. 15, 287-292. doi: 10.1016/0361-9230(85)90153-4.
    • (1985) Brain Res. Bull. , vol.15 , pp. 287-292
    • Banks, W.A.1    Kastin, A.J.2
  • 5
    • 0029871091 scopus 로고    scopus 로고
    • The blood-brain barrier: principles for targeting peptides and drugs to the central nervous system
    • doi: 10.1111/j.2042-7158.1996.tb07112.x
    • Begley, D. J. (1996). The blood-brain barrier: principles for targeting peptides and drugs to the central nervous system. J. Pharm. Pharmacol. 48, 136-146. doi: 10.1111/j.2042-7158.1996.tb07112.x.
    • (1996) J. Pharm. Pharmacol. , vol.48 , pp. 136-146
    • Begley, D.J.1
  • 6
    • 0034729726 scopus 로고    scopus 로고
    • Enkephalin glycopeptide analogues produce analgesia with reduced dependence liability
    • doi: 10.1021/jm000077y
    • Bilsky, E. J., Egleton, R. D., Mitchell, S. A., Palian, M. M., Davis, P., Huber, J. D., et al. (2000). Enkephalin glycopeptide analogues produce analgesia with reduced dependence liability. J. Med. Chem. 43, 2586-2590. doi: 10.1021/jm000077y.
    • (2000) J. Med. Chem. , vol.43 , pp. 2586-2590
    • Bilsky, E.J.1    Egleton, R.D.2    Mitchell, S.A.3    Palian, M.M.4    Davis, P.5    Huber, J.D.6
  • 7
    • 33745107857 scopus 로고    scopus 로고
    • Opioid peptides: synthesis and biological activity of new endomorphin analogues
    • doi: 10.1007/s10989-006-9015-6
    • Biondi, B., Giannini, E., Negri, L., Melchiorri, P., Lattanzi, R., Rosso, F., et al. (2006). Opioid peptides: synthesis and biological activity of new endomorphin analogues. Int. J. Pept. Res. Ther. 12, 145-151. doi: 10.1007/s10989-006-9015-6.
    • (2006) Int. J. Pept. Res. Ther. , vol.12 , pp. 145-151
    • Biondi, B.1    Giannini, E.2    Negri, L.3    Melchiorri, P.4    Lattanzi, R.5    Rosso, F.6
  • 8
    • 84875138812 scopus 로고    scopus 로고
    • Getting in shape: controlling peptide bioactivity and bioavailability using conformational constraints
    • doi: 10.1021/cb300515u
    • Bock, J. E., Gavenonis, J., and Kritzer, J. A. (2013). Getting in shape: controlling peptide bioactivity and bioavailability using conformational constraints. ACS Chem. Biol. 8, 488-499. doi: 10.1021/cb300515u.
    • (2013) ACS Chem. Biol. , vol.8 , pp. 488-499
    • Bock, J.E.1    Gavenonis, J.2    Kritzer, J.A.3
  • 9
    • 1842269785 scopus 로고
    • Transcytotic pathway for blood-borne protein through the blood-brain barrier
    • doi: 10.1073/pnas.85.2.632
    • Broadwell, R. D., Balin, B. J., and Salcman, M. (1988). Transcytotic pathway for blood-borne protein through the blood-brain barrier. Proc. Natl. Acad. Sci. U.S.A. 85, 632-636. doi: 10.1073/pnas.85.2.632.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 632-636
    • Broadwell, R.D.1    Balin, B.J.2    Salcman, M.3
  • 10
    • 33747873262 scopus 로고    scopus 로고
    • Glycopeptides as versatile tools for glycobiology
    • doi: 10.1093/glycob/cwj125
    • Buskas, T., Ingale, S., and Boons, G. J. (2006). Glycopeptides as versatile tools for glycobiology. Glycobiology 16, 113R-136R doi: 10.1093/glycob/cwj125.
    • (2006) Glycobiology , vol.16
    • Buskas, T.1    Ingale, S.2    Boons, G.J.3
  • 11
    • 0028270064 scopus 로고
    • Hydrogen bonding potential as a determinant of the in vitro and in situ blood-brain barrier permeability of peptides
    • doi: 10.1023/A:1018969222130
    • Chikhale, E. G., Ng, K.-Y., Burton, P. S., and Borchardt, R. T. (1994). Hydrogen bonding potential as a determinant of the in vitro and in situ blood-brain barrier permeability of peptides. Pharm Res 11, 412-419. doi: 10.1023/A:1018969222130.
    • (1994) Pharm Res , vol.11 , pp. 412-419
    • Chikhale, E.G.1    Ng, K.-Y.2    Burton, P.S.3    Borchardt, R.T.4
  • 12
    • 77956502216 scopus 로고    scopus 로고
    • The engineering of an orally active conotoxin for the treatment of neuropathic pain
    • doi: 10.1002/anie.201000620
    • Clark, R. J., Jensen, J., Nevin, S. T., Callaghan, B. P., Adams, D. J., and Craik, D. J. (2010). The engineering of an orally active conotoxin for the treatment of neuropathic pain. Angew. Chem. Int. Ed. Engl. 49, 6545-6548. doi: 10.1002/anie.201000620.
    • (2010) Angew. Chem. Int. Ed. Engl. , vol.49 , pp. 6545-6548
    • Clark, R.J.1    Jensen, J.2    Nevin, S.T.3    Callaghan, B.P.4    Adams, D.J.5    Craik, D.J.6
  • 13
    • 80053597731 scopus 로고    scopus 로고
    • Effect of potent endomorphin degradation blockers on analgesic and antidepressant-like responses in mice
    • doi: 10.1016/j.neuropharm.2011.07.021
    • Cravezic, A., Fichna, J., Gach, K., Wyrebska, A., Perlikowska, R., Costentin, J., et al. (2011). Effect of potent endomorphin degradation blockers on analgesic and antidepressant-like responses in mice. Neuropharmacology 61, 1229-1238. doi: 10.1016/j.neuropharm.2011.07.021.
    • (2011) Neuropharmacology , vol.61 , pp. 1229-1238
    • Cravezic, A.1    Fichna, J.2    Gach, K.3    Wyrebska, A.4    Perlikowska, R.5    Costentin, J.6
  • 14
    • 79951557217 scopus 로고    scopus 로고
    • Lipophilic derivatives of leu-enkephalinamide: in vitro permeability, stability and in vivo nasal delivery
    • doi: 10.1016/j.bmc.2010.12.042
    • Cros, C. D., Toth, I., and Blanchfield, J. T. (2011). Lipophilic derivatives of leu-enkephalinamide: in vitro permeability, stability and in vivo nasal delivery. Bioorg. Med. Chem. 19, 1528-1534. doi: 10.1016/j.bmc.2010.12.042.
    • (2011) Bioorg. Med. Chem. , vol.19 , pp. 1528-1534
    • Cros, C.D.1    Toth, I.2    Blanchfield, J.T.3
  • 15
    • 0033835786 scopus 로고    scopus 로고
    • Differential cardiorespiratory effects of endomorphin 1, endomorphin 2, DAMGO, and morphine
    • doi: 10.1164/ajrccm.162.3.9911102
    • Czapla, M. A., Gozal, D., Alea, O. A., Beckerman, R. C., and Zadina, J. E. (2000). Differential cardiorespiratory effects of endomorphin 1, endomorphin 2, DAMGO, and morphine. Am. J. Respir. Crit. Care. Med. 162, 994-999. doi: 10.1164/ajrccm.162.3.9911102.
    • (2000) Am. J. Respir. Crit. Care. Med. , vol.162 , pp. 994-999
    • Czapla, M.A.1    Gozal, D.2    Alea, O.A.3    Beckerman, R.C.4    Zadina, J.E.5
  • 16
    • 70349771755 scopus 로고    scopus 로고
    • TCP-FA4: a derivative of tranylcypromine showing improved blood-brain permeability
    • doi: 10.1016/j.bcp.2009.07.027
    • Desino, K. E., Pignatello, R., Guccione, S., Basile, L., Ansar, S., Michaelis, M. L., et al. (2009). TCP-FA4: a derivative of tranylcypromine showing improved blood-brain permeability. Biochem. Pharmacol. 78, 1412-1417. doi: 10.1016/j.bcp.2009.07.027.
    • (2009) Biochem. Pharmacol. , vol.78 , pp. 1412-1417
    • Desino, K.E.1    Pignatello, R.2    Guccione, S.3    Basile, L.4    Ansar, S.5    Michaelis, M.L.6
  • 17
    • 20244377223 scopus 로고    scopus 로고
    • Glycopeptides related to β-endorphin adopt helical amphipathic conformations in the presence of lipid bilayers
    • doi: 10.1021/ja0432158
    • Dhanasekaran, M., Palian, M. M., Alves, I., Yeomans, L., Keyari, C. M., Davis, P., et al. (2005). Glycopeptides related to β-endorphin adopt helical amphipathic conformations in the presence of lipid bilayers. J. Am. Chem. Soc. 127, 5435-5448. doi: 10.1021/ja0432158.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 5435-5448
    • Dhanasekaran, M.1    Palian, M.M.2    Alves, I.3    Yeomans, L.4    Keyari, C.M.5    Davis, P.6
  • 18
    • 35748943212 scopus 로고    scopus 로고
    • Pharmacologic management of neuropathic pain: evidence-based recommendations
    • doi: 10.1016/j.pain.2007.08.033
    • Dworkin, R. H., O'Connor, A. B., Backonja, M., Farrar, J. T., Finnerup, N. B., Jensen, T. S., et al. (2007). Pharmacologic management of neuropathic pain: evidence-based recommendations. Pain 132, 237-251. doi: 10.1016/j.pain.2007.08.033.
    • (2007) Pain , vol.132 , pp. 237-251
    • Dworkin, R.H.1    O'Connor, A.B.2    Backonja, M.3    Farrar, J.T.4    Finnerup, N.B.5    Jensen, T.S.6
  • 19
    • 0028384750 scopus 로고
    • 'Carbohydrate handles' as natural resources in drug delivery
    • doi: 10.1016/0169-409X(94)90017-5
    • Eduardo, P. (1994). 'Carbohydrate handles' as natural resources in drug delivery. Adv. Drug Delivery Rev. 13, 311-323. doi: 10.1016/0169-409X(94)90017-5.
    • (1994) Adv. Drug Delivery Rev. , vol.13 , pp. 311-323
    • Eduardo, P.1
  • 20
  • 21
    • 12344319635 scopus 로고    scopus 로고
    • Development of neuropeptide drugs that cross the blood-brain barrier
    • doi: 10.1602/neurorx.2.1.44
    • Egleton, R., and Davis, T. (2005). Development of neuropeptide drugs that cross the blood-brain barrier. Neurotherapeutics 2, 44-53. doi: 10.1602/neurorx.2.1.44.
    • (2005) Neurotherapeutics , vol.2 , pp. 44-53
    • Egleton, R.1    Davis, T.2
  • 22
    • 0034693398 scopus 로고    scopus 로고
    • Improved bioavailability to the brain of glycosylated Met-enkephalin analogs
    • doi: 10.1016/S0006-8993(00)02794-3
    • Egleton, R. D., Mitchell, S. A., Huber, J. D., Janders, J., Stropova, D., Polt, R., et al. (2000). Improved bioavailability to the brain of glycosylated Met-enkephalin analogs. Brain Res. 881, 37-46. doi: 10.1016/S0006-8993(00)02794-3.
    • (2000) Brain Res. , vol.881 , pp. 37-46
    • Egleton, R.D.1    Mitchell, S.A.2    Huber, J.D.3    Janders, J.4    Stropova, D.5    Polt, R.6
  • 23
    • 0035200718 scopus 로고    scopus 로고
    • Improved blood-brain barrier penetration and enhanced analgesia of an opioid peptide by glycosylation
    • doi: 10.1602/neurorx.2.1.44
    • Egleton, R. D., Mitchell, S. A., Huber, J. D., Palian, M. M., Polt, R., and Davis, T. P. (2001). Improved blood-brain barrier penetration and enhanced analgesia of an opioid peptide by glycosylation. J. Pharmacol. Exp. Ther. 299, 967-972. doi: 10.1602/neurorx.2.1.44.
    • (2001) J. Pharmacol. Exp. Ther. , vol.299 , pp. 967-972
    • Egleton, R.D.1    Mitchell, S.A.2    Huber, J.D.3    Palian, M.M.4    Polt, R.5    Davis, T.P.6
  • 24
    • 4644258417 scopus 로고    scopus 로고
    • Antinociceptive structure-activity studies with enkephalin-based opioid glycopeptides
    • doi: 10.1124/jpet.104.069393
    • Elmagbari, N. O., Egleton, R. D., Palian, M. M., Lowery, J. J., Schmid, W. R., Davis, P., et al. (2004). Antinociceptive structure-activity studies with enkephalin-based opioid glycopeptides. J. Pharmacol. Exp. Ther. 311, 290-297. doi: 10.1124/jpet.104.069393.
    • (2004) J. Pharmacol. Exp. Ther. , vol.311 , pp. 290-297
    • Elmagbari, N.O.1    Egleton, R.D.2    Palian, M.M.3    Lowery, J.J.4    Schmid, W.R.5    Davis, P.6
  • 25
    • 34748885101 scopus 로고    scopus 로고
    • Design, synthesis and biological evaluation of novel lipoamino acid-based glycolipids for oral drug delivery
    • doi: 10.1016/j.bmc.2007.07.048
    • Falconer, R. A., and Toth, I. (2007). Design, synthesis and biological evaluation of novel lipoamino acid-based glycolipids for oral drug delivery. Bioorg. Med. Chem. 15, 7012-7020. doi: 10.1016/j.bmc.2007.07.048.
    • (2007) Bioorg. Med. Chem. , vol.15 , pp. 7012-7020
    • Falconer, R.A.1    Toth, I.2
  • 26
    • 77952979532 scopus 로고    scopus 로고
    • The novel endomorphin degradation blockers Tyr-Pro-DClPhe-Phe-NH2 (EMDB-1) and Tyr-Pro-Ala-NH2 (EMDB-2) prolong endomorphin-2 action in rat ileum in vitro
    • doi: 10.1111/j.1747-0285.2010.00977.x
    • Fichna, J., Perlikowska, R., Gach, K., do-Rego, J. C., Cravezic, A., Janecka, A., et al. (2010). The novel endomorphin degradation blockers Tyr-Pro-DClPhe-Phe-NH2 (EMDB-1) and Tyr-Pro-Ala-NH2 (EMDB-2) prolong endomorphin-2 action in rat ileum in vitro. Chem. Biol. Drug Des. 76, 77-81. doi: 10.1111/j.1747-0285.2010.00977.x.
    • (2010) Chem. Biol. Drug Des. , vol.76 , pp. 77-81
    • Fichna, J.1    Perlikowska, R.2    Gach, K.3    do-Rego, J.C.4    Cravezic, A.5    Janecka, A.6
  • 27
    • 2142658722 scopus 로고    scopus 로고
    • New trends in the development of opioid peptide analogues as advanced remedies for pain relief
    • doi: 10.2174/1568026043451663
    • Gentilucci, L. (2004). New trends in the development of opioid peptide analogues as advanced remedies for pain relief. Curr. Top. Med. Chem. 4, 19-38. doi: 10.2174/1568026043451663.
    • (2004) Curr. Top. Med. Chem. , vol.4 , pp. 19-38
    • Gentilucci, L.1
  • 28
    • 81255198647 scopus 로고    scopus 로고
    • Opportunities and challenges for oral delivery of hydrophobic versus hydrophilic peptide and protein-like drugs using lipid-based technologies
    • Griffin, B. D., and O'Driscoll, C. M. (2011). Opportunities and challenges for oral delivery of hydrophobic versus hydrophilic peptide and protein-like drugs using lipid-based technologies. Ther. Deliv. 2, 1633-1653.
    • (2011) Ther. Deliv. , vol.2 , pp. 1633-1653
    • Griffin, B.D.1    O'Driscoll, C.M.2
  • 29
    • 0031426851 scopus 로고    scopus 로고
    • Isolation of relatively large amounts of endomorphin-1 and endomorphin-2 from human brain cortex
    • doi: 10.1016/S0196-9781(97)00259-3
    • Hackler, L., Zadina, J. E., Ge, L. J., and Kastin, A. J. (1997). Isolation of relatively large amounts of endomorphin-1 and endomorphin-2 from human brain cortex. Peptides 18, 1635-1639. doi: 10.1016/S0196-9781(97)00259-3.
    • (1997) Peptides , vol.18 , pp. 1635-1639
    • Hackler, L.1    Zadina, J.E.2    Ge, L.J.3    Kastin, A.J.4
  • 30
    • 0001586039 scopus 로고    scopus 로고
    • Opioid peptides and their glycoconjugates: structure-activity relationships
    • Horvat, S. (2001). Opioid peptides and their glycoconjugates: structure-activity relationships. Curr. Med. Chem. 1, 133-154. Available online at: http://dx.doi.org/10.2174/1568015013358581.
    • (2001) Curr. Med. Chem. , vol.1 , pp. 133-154
    • Horvat, S.1
  • 31
    • 0025336463 scopus 로고
    • Emerging approaches in the molecular design of receptor-selective peptide ligands: conformational, topographical and dynamic considerations
    • Hruby, V. J., al-Obeidi, F., and Kazmierski, W. (1990). Emerging approaches in the molecular design of receptor-selective peptide ligands: conformational, topographical and dynamic considerations. Biochem. J. 268, 249-262.
    • (1990) Biochem. J. , vol.268 , pp. 249-262
    • Hruby, V.J.1    al-Obeidi, F.2    Kazmierski, W.3
  • 32
    • 0033851469 scopus 로고    scopus 로고
    • Conformational and topographical considerations in designing agonist peptidomimetics from peptide leads
    • doi: 10.2174/0929867003374499
    • Hruby, V. J., and Balse, P. M. (2000). Conformational and topographical considerations in designing agonist peptidomimetics from peptide leads. Curr. Med. Chem. 7, 945-970. doi: 10.2174/0929867003374499.
    • (2000) Curr. Med. Chem. , vol.7 , pp. 945-970
    • Hruby, V.J.1    Balse, P.M.2
  • 33
    • 0016701344 scopus 로고
    • Identification of two related pentapeptides from the brain with potent opiate agonist activity
    • doi: 10.1038/258577a0
    • Hughes, J., Smith, T. W., Kosterlitz, H. W., Fothergill, L. A., Morgan, B. A., and Morris, H. R. (1975). Identification of two related pentapeptides from the brain with potent opiate agonist activity. Nature 258, 577-580. doi: 10.1038/258577a0.
    • (1975) Nature , vol.258 , pp. 577-580
    • Hughes, J.1    Smith, T.W.2    Kosterlitz, H.W.3    Fothergill, L.A.4    Morgan, B.A.5    Morris, H.R.6
  • 34
    • 33746305665 scopus 로고    scopus 로고
    • Potent in vivo antinociception and opioid receptor preference of the novel analogue [Dmt1]endomorphin-1
    • doi: 10.1016/j.pbb.2006.05.005
    • Jinsmaa, Y., Marczak, E., Fujita, Y., Shiotani, K., Miyazaki, A., Li, T., et al. (2006). Potent in vivo antinociception and opioid receptor preference of the novel analogue [Dmt1]endomorphin-1. Pharmacol. Biochem. Behav. 84, 252-258. doi: 10.1016/j.pbb.2006.05.005.
    • (2006) Pharmacol. Biochem. Behav. , vol.84 , pp. 252-258
    • Jinsmaa, Y.1    Marczak, E.2    Fujita, Y.3    Shiotani, K.4    Miyazaki, A.5    Li, T.6
  • 35
    • 0033578005 scopus 로고    scopus 로고
    • G-protein-coupled receptor heterodimerization modulates receptor function
    • doi: 10.1038/21441
    • Jordan, B. A., and Devi, L. A. (1999). G-protein-coupled receptor heterodimerization modulates receptor function. Nature 399, 697-700. doi: 10.1038/21441.
    • (1999) Nature , vol.399 , pp. 697-700
    • Jordan, B.A.1    Devi, L.A.2
  • 36
    • 0025324011 scopus 로고
    • Preparation and opioid activities of N-methylated analogs of [D-Ala2,Leu5]enkephalin
    • doi: 10.1111/j.1399-3011.1990.tb00072.x
    • Kawai, M., Fukuta, N., Ito, N., Kagami, T., Butsugan, Y., Maruyama, M., et al. (1990). Preparation and opioid activities of N-methylated analogs of [D-Ala2,Leu5]enkephalin. Int. J. Pept. Protein Res. 35, 452-459. doi: 10.1111/j.1399-3011.1990.tb00072.x.
    • (1990) Int. J. Pept. Protein Res. , vol.35 , pp. 452-459
    • Kawai, M.1    Fukuta, N.2    Ito, N.3    Kagami, T.4    Butsugan, Y.5    Maruyama, M.6
  • 37
    • 44449179814 scopus 로고    scopus 로고
    • Synthesis and in vitro evaluation of a library of modified endomorphin 1 peptides
    • doi: 10.1016/j.bmc.2008.04.020
    • Koda, Y., Del Borgo, M., Wessling, S. T., Lazarus, L. H., Okada, Y., Toth, I., et al. (2008). Synthesis and in vitro evaluation of a library of modified endomorphin 1 peptides. Bioorg. Med. Chem. 16, 6286-6296. doi: 10.1016/j.bmc.2008.04.020.
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 6286-6296
    • Koda, Y.1    Del Borgo, M.2    Wessling, S.T.3    Lazarus, L.H.4    Okada, Y.5    Toth, I.6
  • 38
    • 0029857593 scopus 로고    scopus 로고
    • Synthesis of medicinally useful lipidicalpha-amino acids, 2-amino alcohols and diamines
    • doi: 10.1007/BF00807940
    • Kokotos, G., Martin, V., Constantinou-Kokotou, V., and Gibbons, W. A. (1996). Synthesis of medicinally useful lipidicalpha-amino acids, 2-amino alcohols and diamines. Amino Acids 11, 329-343. doi: 10.1007/BF00807940.
    • (1996) Amino Acids , vol.11 , pp. 329-343
    • Kokotos, G.1    Martin, V.2    Constantinou-Kokotou, V.3    Gibbons, W.A.4
  • 39
    • 84855489807 scopus 로고    scopus 로고
    • (Inventor). Patent Number: WO2003090697 US.
    • Kream, R. M. (Inventor). (2003). Chimeric Hybrid Analgesics. Patent Number: WO2003090697 US.
    • (2003) Chimeric Hybrid Analgesics
    • Kream, R.M.1
  • 40
    • 33846925112 scopus 로고    scopus 로고
    • Synthesis and pharmacological analysis of a morphine/substance P chimeric molecule with full analgesic potency in morphine-tolerant rats
    • Kream, R. M., Liu, N. L., Zhuang, M., Esposito, P. L., Esposito, T. R., Stefano, G. B., et al. (2007). Synthesis and pharmacological analysis of a morphine/substance P chimeric molecule with full analgesic potency in morphine-tolerant rats. Med. Sci. Monit. 13, BR25-BR31.
    • (2007) Med. Sci. Monit. , vol.13
    • Kream, R.M.1    Liu, N.L.2    Zhuang, M.3    Esposito, P.L.4    Esposito, T.R.5    Stefano, G.B.6
  • 41
    • 0036462451 scopus 로고    scopus 로고
    • Oligomerization of opioid receptors: generation of novel signaling units
    • doi: 10.1016/S1471-4892(02)00124-8
    • Levac, B. A., O'Dowd, B. F., and George, S. R. (2002). Oligomerization of opioid receptors: generation of novel signaling units. Curr. Opin. Pharmacol. 2, 76-81. doi: 10.1016/S1471-4892(02)00124-8.
    • (2002) Curr. Opin. Pharmacol. , vol.2 , pp. 76-81
    • Levac, B.A.1    O'Dowd, B.F.2    George, S.R.3
  • 42
    • 19944433385 scopus 로고    scopus 로고
    • Development of potent mu-opioid receptor ligands using unique tyrosine analogues of endomorphin-2
    • doi: 10.1021/jm049384k
    • Li, T. Y., Fujita, Y., Tsuda, Y., Miyazaki, A., Ambo, A., Sasaki, Y., et al. (2005). Development of potent mu-opioid receptor ligands using unique tyrosine analogues of endomorphin-2. J. Med. Chem. 48, 586-592. doi: 10.1021/jm049384k.
    • (2005) J. Med. Chem. , vol.48 , pp. 586-592
    • Li, T.Y.1    Fujita, Y.2    Tsuda, Y.3    Miyazaki, A.4    Ambo, A.5    Sasaki, Y.6
  • 43
    • 0032971927 scopus 로고    scopus 로고
    • Dermorphin and deltorphin glycosylated analogues:? synthesis and antinociceptive activity after systemic administration
    • doi: 10.1021/jm9810699
    • Negri, L., Lattanzi, R., Tabacco, F., Orru, L., Severini, C., Scolaro, B., et al. (1999). Dermorphin and deltorphin glycosylated analogues:? synthesis and antinociceptive activity after systemic administration. J. Med. Chem. 42, 400-404. doi: 10.1021/jm9810699.
    • (1999) J. Med. Chem. , vol.42 , pp. 400-404
    • Negri, L.1    Lattanzi, R.2    Tabacco, F.3    Orru, L.4    Severini, C.5    Scolaro, B.6
  • 44
    • 0038296015 scopus 로고    scopus 로고
    • Glycopeptide-membrane interactions: glycosyl enkephalin analogues adopt turn conformations by NMR and CD in amphipathic media
    • doi: 10.1021/ja0268635
    • Palian, M. M., Boguslavsky, V. I., O'Brie, D. F., and Polt, R. (2003). Glycopeptide-membrane interactions: glycosyl enkephalin analogues adopt turn conformations by NMR and CD in amphipathic media. J. Am. Chem. Soc. 125, 5823-5831. doi: 10.1021/ja0268635.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 5823-5831
    • Palian, M.M.1    Boguslavsky, V.I.2    O'Brie, D.F.3    Polt, R.4
  • 45
    • 26844487072 scopus 로고    scopus 로고
    • Enhancement of drug affinity for cell membranes by conjugation with lipoamino acids. I. Synthesis and biological evaluation of lipophilic conjugates of tranylcypromine
    • doi: 10.1016/j.ejmech.2005.05.009
    • Pignatello, R., Puleo, A., Guccione, S., Raciti, G., Acquaviva, R., Campisi, A., et al. (2005). Enhancement of drug affinity for cell membranes by conjugation with lipoamino acids. I. Synthesis and biological evaluation of lipophilic conjugates of tranylcypromine. Eur. J. Med. Chem. 40, 1074-1079. doi: 10.1016/j.ejmech.2005.05.009.
    • (2005) Eur. J. Med. Chem. , vol.40 , pp. 1074-1079
    • Pignatello, R.1    Puleo, A.2    Guccione, S.3    Raciti, G.4    Acquaviva, R.5    Campisi, A.6
  • 46
    • 0028273935 scopus 로고
    • Glycation increases the permeability of proteins across the blood-nerve and blood-brain barriers
    • doi: 10.1016/0169-328X(94)90222-4
    • Poduslo, J. F., and Curran, G. L. (1994). Glycation increases the permeability of proteins across the blood-nerve and blood-brain barriers. Brain. Res. Mol. Brain Res. 23, 157-162. doi: 10.1016/0169-328X(94)90222-4.
    • (1994) Brain. Res. Mol. Brain Res. , vol.23 , pp. 157-162
    • Poduslo, J.F.1    Curran, G.L.2
  • 48
    • 24144479258 scopus 로고    scopus 로고
    • Glycosylated neuropeptides: a new vista for neuropsychopharmacology?
    • doi: 10.1002/med.20039
    • Polt, R., Dhanasekaran, M., and Keyari, C. M. (2005b). Glycosylated neuropeptides: a new vista for neuropsychopharmacology? Med. Res. Rev. 25, 557-585. doi: 10.1002/med.20039.
    • (2005) Med. Res. Rev. , vol.25 , pp. 557-585
    • Polt, R.1    Dhanasekaran, M.2    Keyari, C.M.3
  • 49
    • 84891679125 scopus 로고    scopus 로고
    • Biomedicine of enkephalin-derived glycopeptide analgesics
    • eds B. Fraser-Reid, K. Tatsuta, J. Thiem (Berlin; Heidelberg: Springer). doi: 10.1007/978-3-540-30429-6_65.
    • Polt, R. (2008). "Biomedicine of enkephalin-derived glycopeptide analgesics," in Glycoscience eds B. Fraser-Reid, K. Tatsuta, J. Thiem (Berlin; Heidelberg: Springer), 2525-2543. doi: 10.1007/978-3-540-30429-6_65.
    • (2008) Glycoscience , pp. 2525-2543
    • Polt, R.1
  • 50
    • 0028233389 scopus 로고
    • Glycopeptide enkephalin analogues produce analgesia in mice: evidence for penetration of the blood-brain barrier
    • doi: 10.1073/pnas.91.15.7114
    • Polt, R., Porreca, F., Szabo, L. Z., Bilsky, E. J., Davis, P., Abbruscato, T. J., et al. (1994). Glycopeptide enkephalin analogues produce analgesia in mice: evidence for penetration of the blood-brain barrier. Proc. Natl. Acad. Sci. U.S.A. 91, 7114-7118. doi: 10.1073/pnas.91.15.7114.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 7114-7118
    • Polt, R.1    Porreca, F.2    Szabo, L.Z.3    Bilsky, E.J.4    Davis, P.5    Abbruscato, T.J.6
  • 51
    • 0035840823 scopus 로고    scopus 로고
    • Opioids in chronic pain
    • doi: 10.1016/S0014-2999(01)01308-5
    • Przewlocki, R., and Przewlocka, B. (2001). Opioids in chronic pain. Eur. J. Pharmacol. 429, 79-91. doi: 10.1016/S0014-2999(01)01308-5.
    • (2001) Eur. J. Pharmacol. , vol.429 , pp. 79-91
    • Przewlocki, R.1    Przewlocka, B.2
  • 52
    • 0142039133 scopus 로고    scopus 로고
    • Degradation of endomorphin-2 at the supraspinal level in mice is initiated by dipeptidyl peptidase IV: an in vitro and in vivo study
    • doi: 10.1016/S0006-2952(03)00391-5
    • Sakurada, C., Sakurada, S., Hayashi, T., Katsuyama, S., Tan-No, K., and Sakurada, T. (2003). Degradation of endomorphin-2 at the supraspinal level in mice is initiated by dipeptidyl peptidase IV: an in vitro and in vivo study. Biochem. Pharmacol. 66, 653-661. doi: 10.1016/S0006-2952(03)00391-5.
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 653-661
    • Sakurada, C.1    Sakurada, S.2    Hayashi, T.3    Katsuyama, S.4    Tan-No, K.5    Sakurada, T.6
  • 53
    • 0020471764 scopus 로고
    • Opiate receptor subclasses differ in their conformational requirements
    • doi: 10.1038/297074a0
    • Schiller, P. W., and DiMaio, J. (1982). Opiate receptor subclasses differ in their conformational requirements. Nature 297, 74-76. doi: 10.1038/297074a0.
    • (1982) Nature , vol.297 , pp. 74-76
    • Schiller, P.W.1    DiMaio, J.2
  • 54
    • 35448990534 scopus 로고    scopus 로고
    • Lipidated peptides as tools for understanding the membrane interactions of lipid-modified proteins
    • doi: 10.1016/S1063-5823(02)52015-9
    • Silvius, J. R. (2002). Lipidated peptides as tools for understanding the membrane interactions of lipid-modified proteins. Curr. Top. Membr. 52, 371-95. doi: 10.1016/S1063-5823(02)52015-9.
    • (2002) Curr. Top. Membr. , vol.52 , pp. 371-95
    • Silvius, J.R.1
  • 57
    • 0028067744 scopus 로고
    • A novel chemical approach to drug delivery: lipidic amino acid conjugates
    • doi: 10.3109/10611869408996805
    • Toth, I. (1994). A novel chemical approach to drug delivery: lipidic amino acid conjugates. J. Drug Target. 2, 217-239. doi: 10.3109/10611869408996805.
    • (1994) J. Drug Target. , vol.2 , pp. 217-239
    • Toth, I.1
  • 58
    • 0034534528 scopus 로고    scopus 로고
    • Endogenous opiates: 1999
    • doi: 10.1016/S0196-9781(00)00345-4
    • Vaccarino, A. L., and Kastin, A. J. (2000). Endogenous opiates: 1999. Peptides 21, 1975-2034. doi: 10.1016/S0196-9781(00)00345-4.
    • (2000) Peptides , vol.21 , pp. 1975-2034
    • Vaccarino, A.L.1    Kastin, A.J.2
  • 59
    • 0033395852 scopus 로고    scopus 로고
    • Endogenous opiates: 1998
    • doi: 10.1016/S0196-9781(99)00166-7
    • Vaccarino, A. L., Olson, G. A., Olson, R. D., and Kastin, A. J. (1999). Endogenous opiates: 1998. Peptides 20, 1527-1574. doi: 10.1016/S0196-9781(99)00166-7.
    • (1999) Peptides , vol.20 , pp. 1527-1574
    • Vaccarino, A.L.1    Olson, G.A.2    Olson, R.D.3    Kastin, A.J.4
  • 60
    • 84875227905 scopus 로고    scopus 로고
    • Peripherally acting novel lipo-endomorphin-1 peptides in neuropathic pain without producing constipation
    • doi: 10.1016/j.bmc.2013.01.044
    • Varamini, P., Goh, W. H., Mansfeld, F. M., Blanchfield, J. T., Wyse, B. D., Smith, M. T., et al. (2013). Peripherally acting novel lipo-endomorphin-1 peptides in neuropathic pain without producing constipation. Bioorg. Med. Chem. 21, 1898-1904. doi: 10.1016/j.bmc.2013.01.044.
    • (2013) Bioorg. Med. Chem. , vol.21 , pp. 1898-1904
    • Varamini, P.1    Goh, W.H.2    Mansfeld, F.M.3    Blanchfield, J.T.4    Wyse, B.D.5    Smith, M.T.6
  • 61
    • 84867580402 scopus 로고    scopus 로고
    • Synthesis, biological activity and structure-activity relationship of endomorphin-1/substance P derivatives
    • doi: 10.1016/j.bmc.2012.09.003
    • Varamini, P., Hussein, W. M., Mansfeld, F. M., and Toth, I. (2012a). Synthesis, biological activity and structure-activity relationship of endomorphin-1/substance P derivatives. Bioorg. Med. Chem. 20, 6335-6343. doi: 10.1016/j.bmc.2012.09.003.
    • (2012) Bioorg. Med. Chem. , vol.20 , pp. 6335-6343
    • Varamini, P.1    Hussein, W.M.2    Mansfeld, F.M.3    Toth, I.4
  • 62
    • 84865095335 scopus 로고    scopus 로고
    • Lipo-endomorphin-1 derivatives with systemic activity against neuropathic pain without producing constipation
    • doi: 10.1371/journal.pone.0041909.
    • Varamini, P., Mansfeld, F. M., Blanchfield, J. T., Wyse, B. D., Smith, M. T., and Toth, I. (2012b). Lipo-endomorphin-1 derivatives with systemic activity against neuropathic pain without producing constipation. PLoS ONE 7:e41909. doi: 10.1371/journal.pone.0041909.
    • (2012) PLoS ONE , vol.7
    • Varamini, P.1    Mansfeld, F.M.2    Blanchfield, J.T.3    Wyse, B.D.4    Smith, M.T.5    Toth, I.6
  • 63
    • 84863092840 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of an orally active glycosylated endomorphin-1
    • doi: 10.1021/jm300418d
    • Varamini, P., Mansfeld, F. M., Blanchfield, J. T., Wyse, B. D., Smith, M. T., and Toth, I. (2012c). Synthesis and biological evaluation of an orally active glycosylated endomorphin-1. J. Med. Chem. 55, 5859-5867. doi: 10.1021/jm300418d.
    • (2012) J. Med. Chem. , vol.55 , pp. 5859-5867
    • Varamini, P.1    Mansfeld, F.M.2    Blanchfield, J.T.3    Wyse, B.D.4    Smith, M.T.5    Toth, I.6
  • 64
    • 33745083089 scopus 로고    scopus 로고
    • Reversible lipidization for the oral delivery of leu-enkephalin
    • doi: 10.1080/10611860600648221
    • Wang, J., Hogenkamp, D. J., Tran, M., Li, W. Y., Yoshimura, R. F., Johnstone, T. B. C., et al. (2006). Reversible lipidization for the oral delivery of leu-enkephalin. J. Drug. Target. 14, 127-136. doi: 10.1080/10611860600648221.
    • (2006) J. Drug. Target. , vol.14 , pp. 127-136
    • Wang, J.1    Hogenkamp, D.J.2    Tran, M.3    Li, W.Y.4    Yoshimura, R.F.5    Johnstone, T.B.C.6
  • 67
    • 0037267005 scopus 로고    scopus 로고
    • Glucose transporters (GLUT and SGLT): expanded families of sugar transport proteins
    • doi: 10.1079/BJN2002763
    • Wood, I. S., and Trayhurn, P. (2003). Glucose transporters (GLUT and SGLT): expanded families of sugar transport proteins. The British journal of nutrition 89, 3-9. doi: 10.1079/BJN2002763.
    • (2003) The British journal of nutrition , vol.89 , pp. 3-9
    • Wood, I.S.1    Trayhurn, P.2
  • 68
    • 0030933655 scopus 로고    scopus 로고
    • A potent and selective endogenous agonist for the μ-opiate receptor
    • doi: 10.1038/386499a0
    • Zadina, J. E., Hackler, L., Ge, L.-J., and Kastin, A. J. (1997). A potent and selective endogenous agonist for the μ-opiate receptor. Nature 386, 499-502. doi: 10.1038/386499a0.
    • (1997) Nature , vol.386 , pp. 499-502
    • Zadina, J.E.1    Hackler, L.2    Ge, L.-J.3    Kastin, A.J.4


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