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Volumn 8, Issue 3, 2013, Pages 488-499

Getting in shape: Controlling peptide bioactivity and bioavailability using conformational constraints

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ALKENE; ALPHA AMANITIN; CALCIUM CHANNEL BLOCKING AGENT; CYCLOSPORIN A; ENFUVIRTIDE; ENKEPHALIN; FIBRONECTIN; GABAPENTIN; GLYCINE; GROWTH HORMONE; KALATA B1; MELANOCORTIN; NATURAL PRODUCT; OXYTOCIN; PARATHYROID HORMONE RELATED PROTEIN; PHENYLALANINE; PROTEIN BCL 2; SOMATOSTATIN; SOMATOSTATIN DERIVATIVE; UNCLASSIFIED DRUG; PEPTIDE;

EID: 84875138812     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb300515u     Document Type: Review
Times cited : (187)

References (145)
  • 1
    • 0031024171 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • Lipinski, C. A., Lombardo, F., Dominy, B. W., and Feeney, P. J. (1997) Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings Adv. Drug Delivery Rev. 23, 3-25
    • (1997) Adv. Drug Delivery Rev. , vol.23 , pp. 3-25
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 2
    • 0037030653 scopus 로고    scopus 로고
    • Molecular properties that influence the oral bioavailability of drug candidates
    • Veber, D. F., Johnson, S. R., Cheng, H. Y., Smith, B. R., Ward, K. W., and Kopple, K. D. (2002) Molecular properties that influence the oral bioavailability of drug candidates J. Med. Chem. 45, 2615-2623
    • (2002) J. Med. Chem. , vol.45 , pp. 2615-2623
    • Veber, D.F.1    Johnson, S.R.2    Cheng, H.Y.3    Smith, B.R.4    Ward, K.W.5    Kopple, K.D.6
  • 3
    • 46449115901 scopus 로고    scopus 로고
    • The exploration of macrocycles for drug discovery - An underexploited structural class
    • Driggers, E. M., Hale, S. P., Lee, J., and Terrett, N. K. (2008) The exploration of macrocycles for drug discovery-an underexploited structural class Nat. Rev. Drug Discovery 7, 608-624
    • (2008) Nat. Rev. Drug Discovery , vol.7 , pp. 608-624
    • Driggers, E.M.1    Hale, S.P.2    Lee, J.3    Terrett, N.K.4
  • 5
    • 36749018204 scopus 로고    scopus 로고
    • Privileged structures: A useful concept for the rational design of new lead drug candidates
    • Duarte, C. D., Barreiro, E. J., and Fraga, C. A. M. (2007) Privileged structures: A useful concept for the rational design of new lead drug candidates Mini-Rev. Med. Chem. 7, 1108-1119
    • (2007) Mini-Rev. Med. Chem. , vol.7 , pp. 1108-1119
    • Duarte, C.D.1    Barreiro, E.J.2    Fraga, C.A.M.3
  • 6
    • 0141460364 scopus 로고
    • On the influence of intravenous injections of an extract of the pancreas on experimental pancreatic diabetes
    • Scott, E. L. (1912) On the influence of intravenous injections of an extract of the pancreas on experimental pancreatic diabetes Am. J. Physiol. 29, 306-310
    • (1912) Am. J. Physiol. , vol.29 , pp. 306-310
    • Scott, E.L.1
  • 8
    • 0036257686 scopus 로고    scopus 로고
    • Converting a peptide into a drug: Strategies to improve stability and bioavailability
    • Adessi, C. and Soto, C. (2002) Converting a peptide into a drug: Strategies to improve stability and bioavailability Curr. Med. Chem. 9, 963-978
    • (2002) Curr. Med. Chem. , vol.9 , pp. 963-978
    • Adessi, C.1    Soto, C.2
  • 9
    • 44949231073 scopus 로고    scopus 로고
    • Peptidomimetics, a synthetic tool of drug discovery
    • Vagner, J., Qu, H. C., and Hruby, V. J. (2008) Peptidomimetics, a synthetic tool of drug discovery Curr. Opin. Chem. Biol. 12, 292-296
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 292-296
    • Vagner, J.1    Qu, H.C.2    Hruby, V.J.3
  • 10
    • 0018111845 scopus 로고
    • Amatoxins, phallotoxins, phallolysin, and antamanide - Biologically-active components of poisonous amanita mushrooms
    • Wieland, T. and Faulstich, H. (1978) Amatoxins, phallotoxins, phallolysin, and antamanide-biologically-active components of poisonous amanita mushrooms CRC Crit. Rev. Biochem. 5, 185-260
    • (1978) CRC Crit. Rev. Biochem. , vol.5 , pp. 185-260
    • Wieland, T.1    Faulstich, H.2
  • 12
    • 0025885621 scopus 로고
    • 50 years of amanitin
    • Wieland, T. and Faulstich, H. (1991) 50 years of amanitin Experientia 47, 1186-1193
    • (1991) Experientia , vol.47 , pp. 1186-1193
    • Wieland, T.1    Faulstich, H.2
  • 13
    • 33645806523 scopus 로고    scopus 로고
    • Molecular characterization and inhibition of amanitin uptake into human hepatocytes
    • Letschert, K., Faulstich, H., Keller, D., and Keppler, D. (2006) Molecular characterization and inhibition of amanitin uptake into human hepatocytes Toxicol. Sci. 91, 140-149
    • (2006) Toxicol. Sci. , vol.91 , pp. 140-149
    • Letschert, K.1    Faulstich, H.2    Keller, D.3    Keppler, D.4
  • 14
    • 0014959969 scopus 로고
    • Specific inhibition of nuclear RNA polymerase II by alpha-amanitin
    • Lindell, T. J., Weinberg, F., Morris, P. W., Roeder, R. G., and Rutter, W. J. (1970) Specific inhibition of nuclear RNA polymerase II by alpha-amanitin Science 170, 447-449
    • (1970) Science , vol.170 , pp. 447-449
    • Lindell, T.J.1    Weinberg, F.2    Morris, P.W.3    Roeder, R.G.4    Rutter, W.J.5
  • 15
    • 0026575932 scopus 로고
    • The mechanism of action of cyclosporine-A and FK506
    • Schreiber, S. L. and Crabtree, G. R. (1992) The mechanism of action of cyclosporine-A and FK506 Immunol. Today 13, 136-142
    • (1992) Immunol. Today , vol.13 , pp. 136-142
    • Schreiber, S.L.1    Crabtree, G.R.2
  • 16
    • 0028273057 scopus 로고
    • The 3D structure of a cyclosporine analog in water is nearly identical to the cyclophilin-bound cyclosporine conformation
    • Wenger, R. M., France, J., Bovermann, G., Walliser, L., Widmer, A., and Widmer, H. (1994) The 3D structure of a cyclosporine analog in water is nearly identical to the cyclophilin-bound cyclosporine conformation FEBS Lett. 340, 255-259
    • (1994) FEBS Lett. , vol.340 , pp. 255-259
    • Wenger, R.M.1    France, J.2    Bovermann, G.3    Walliser, L.4    Widmer, A.5    Widmer, H.6
  • 17
    • 0026532051 scopus 로고
    • A conformation of cyclosporine-A in aqueous environment revealed by the X-ray structure of a cyclosporine-FAB complex
    • Altschuh, D., Vix, O., Rees, B., and Thierry, J. C. (1992) A conformation of cyclosporine-A in aqueous environment revealed by the X-ray structure of a cyclosporine-FAB complex Science 256, 92-94
    • (1992) Science , vol.256 , pp. 92-94
    • Altschuh, D.1    Vix, O.2    Rees, B.3    Thierry, J.C.4
  • 19
    • 0026686692 scopus 로고
    • A model of the cyclophilin cyclosporine-A (CSA) complex from NMR and X-ray data suggests that CSA binds as a transition-state analog
    • Fesik, S. W., Neri, P., Meadows, R., Olejniczak, E. T., and Gemmecker, G. (1992) A model of the cyclophilin cyclosporine-A (CSA) complex from NMR and X-ray data suggests that CSA binds as a transition-state analog J. Am. Chem. Soc. 114, 3165-3166
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 3165-3166
    • Fesik, S.W.1    Neri, P.2    Meadows, R.3    Olejniczak, E.T.4    Gemmecker, G.5
  • 20
    • 0025858482 scopus 로고
    • Structure of human cyclophilin and its binding-site for cyclosporine-A determined by X-ray crystallography and NMR spectroscopy
    • Kallen, J., Spitzfaden, C., Zurini, M. G. M., Wider, G., Widmer, H., Wuthrich, K., and Walkinshaw, M. D. (1991) Structure of human cyclophilin and its binding-site for cyclosporine-A determined by X-ray crystallography and NMR spectroscopy Nature 353, 276-279
    • (1991) Nature , vol.353 , pp. 276-279
    • Kallen, J.1    Spitzfaden, C.2    Zurini, M.G.M.3    Wider, G.4    Widmer, H.5    Wuthrich, K.6    Walkinshaw, M.D.7
  • 22
    • 0025054575 scopus 로고
    • Reinvestigation of the conformation of cyclosporine-A in chloroform
    • Kessler, H., Kock, M., Wein, T., and Gehrke, M. (1990) Reinvestigation of the conformation of cyclosporine-A in chloroform Helv. Chim. Acta 73, 1818-1832
    • (1990) Helv. Chim. Acta , vol.73 , pp. 1818-1832
    • Kessler, H.1    Kock, M.2    Wein, T.3    Gehrke, M.4
  • 23
    • 0001334658 scopus 로고    scopus 로고
    • Design principles for orally bioavailable drugs
    • Navia, M. A. and Chaturvedi, P. R. (1996) Design principles for orally bioavailable drugs Drug Discovery Today 1, 179-189
    • (1996) Drug Discovery Today , vol.1 , pp. 179-189
    • Navia, M.A.1    Chaturvedi, P.R.2
  • 25
    • 33750482579 scopus 로고    scopus 로고
    • Conformational flexibility, internal hydrogen bonding, and passive membrane permeability: Successful in silico prediction of the relative permeabilities of cyclic peptides
    • Rezai, T., Bock, J. E., Zhou, M. V., Kalyanaraman, C., Lokey, R. S., and Jacobson, M. P. (2006) Conformational flexibility, internal hydrogen bonding, and passive membrane permeability: Successful in silico prediction of the relative permeabilities of cyclic peptides J. Am. Chem. Soc. 128, 14073-14080
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 14073-14080
    • Rezai, T.1    Bock, J.E.2    Zhou, M.V.3    Kalyanaraman, C.4    Lokey, R.S.5    Jacobson, M.P.6
  • 26
    • 57349171593 scopus 로고    scopus 로고
    • N-Methylation of peptides: A new perspective in medicinal chemistry
    • Chatterjee, J., Gilon, C., Hoffman, A., and Kessler, H. (2008) N-Methylation of peptides: a new perspective in medicinal chemistry Acc. Chem. Res. 41, 1331-1342
    • (2008) Acc. Chem. Res. , vol.41 , pp. 1331-1342
    • Chatterjee, J.1    Gilon, C.2    Hoffman, A.3    Kessler, H.4
  • 29
    • 0033851469 scopus 로고    scopus 로고
    • Conformational and topographical considerations in designing agonist peptidomimetics from peptide leads
    • 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
    • (2000) Curr. Med. Chem. , vol.7 , pp. 945-970
    • Hruby, V.J.1    Balse, P.M.2
  • 30
    • 0025336463 scopus 로고
    • Emerging approaches in the molecular design of receptor-selective peptide ligands - Conformational, topographical and dynamic considerations
    • Hruby, V. J., Alobeidi, 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    Alobeidi, F.2    Kazmierski, W.3
  • 31
    • 0020163940 scopus 로고
    • Peptide conformations 0.19. Conformation and biological-activity of cyclic-peptides
    • Kessler, H. (1982) Peptide conformations 0.19. Conformation and biological-activity of cyclic-peptides Angew. Chem., Int. Ed. Engl. 21, 512-523
    • (1982) Angew. Chem., Int. Ed. Engl. , vol.21 , pp. 512-523
    • Kessler, H.1
  • 34
    • 0019163001 scopus 로고
    • Bioactive conformation of luteinizing-hormone-releasing hormone - Evidence from a conformationally constrained analog
    • Freidinger, R. M., Veber, D. F., Perlow, D. S., Brooks, J. R., and Saperstein, R. (1980) Bioactive conformation of luteinizing-hormone-releasing hormone-evidence from a conformationally constrained analog Science 210, 656-658
    • (1980) Science , vol.210 , pp. 656-658
    • Freidinger, R.M.1    Veber, D.F.2    Perlow, D.S.3    Brooks, J.R.4    Saperstein, R.5
  • 37
    • 0024310869 scopus 로고
    • Potent and prolonged acting cyclic lactam analogues of alpha-melanotropin: Design based on molecular dynamics
    • Al-Obeidi, F., Castrucci, A. M., Hadley, M. E., and Hruby, V. J. (1989) Potent and prolonged acting cyclic lactam analogues of alpha-melanotropin: design based on molecular dynamics J. Med. Chem. 32, 2555-2561
    • (1989) J. Med. Chem. , vol.32 , pp. 2555-2561
    • Al-Obeidi, F.1    Castrucci, A.M.2    Hadley, M.E.3    Hruby, V.J.4
  • 38
    • 77953304018 scopus 로고    scopus 로고
    • Multiple N-methylation of MT-II backbone amide bonds leads to melanocortin receptor subtype hMC1R selectivity: Pharmacological and conformational studies
    • Doedens, L., Opperer, F., Cai, M., Beck, J. G., Dedek, M., Palmer, E., Hruby, V. J., and Kessler, H. (2010) Multiple N-methylation of MT-II backbone amide bonds leads to melanocortin receptor subtype hMC1R selectivity: pharmacological and conformational studies J. Am. Chem. Soc. 132, 8115-8128
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 8115-8128
    • Doedens, L.1    Opperer, F.2    Cai, M.3    Beck, J.G.4    Dedek, M.5    Palmer, E.6    Hruby, V.J.7    Kessler, H.8
  • 39
    • 58149194055 scopus 로고    scopus 로고
    • Structure-activity relationship and metabolic stability studies of backbone cyclization and N-methylation of melanocortin peptides
    • Linde, Y., Ovadia, O., Safrai, E., Xiang, Z., Portillo, F. P., Shalev, D. E., Haskell-Luevano, C., Hoffman, A., and Gilon, C. (2008) Structure-activity relationship and metabolic stability studies of backbone cyclization and N-methylation of melanocortin peptides Biopolymers 90, 671-682
    • (2008) Biopolymers , vol.90 , pp. 671-682
    • Linde, Y.1    Ovadia, O.2    Safrai, E.3    Xiang, Z.4    Portillo, F.P.5    Shalev, D.E.6    Haskell-Luevano, C.7    Hoffman, A.8    Gilon, C.9
  • 40
    • 0024551431 scopus 로고
    • Design of a new class of superpotent cyclic.alpha.-melanotropins based on quenched dynamic simulations
    • Al-Obeidi, F., Hadley, M. E., Pettitt, B. M., and Hruby, V. J. (1989) Design of a new class of superpotent cyclic.alpha.-melanotropins based on quenched dynamic simulations J. Am. Chem. Soc. 111, 3413-3416
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 3413-3416
    • Al-Obeidi, F.1    Hadley, M.E.2    Pettitt, B.M.3    Hruby, V.J.4
  • 42
    • 0019848776 scopus 로고
    • Location of the cell-attachment site in fibronectin with monoclonal antibodies and proteolytic fragments of the molecule
    • Pierschbacher, M. D., Hayman, E. G., and Ruoslahti, E. (1981) Location of the cell-attachment site in fibronectin with monoclonal antibodies and proteolytic fragments of the molecule Cell 26, 259-267
    • (1981) Cell , vol.26 , pp. 259-267
    • Pierschbacher, M.D.1    Hayman, E.G.2    Ruoslahti, E.3
  • 43
    • 0021271957 scopus 로고
    • Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
    • Pierschbacher, M. D. and Ruoslahti, E. (1984) Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule Nature 309, 30-33
    • (1984) Nature , vol.309 , pp. 30-33
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 44
    • 0025880146 scopus 로고
    • Arg-Gly-Asp constrained within cyclic pentapeptides - Strong and selective inhibitors of cell-adhesion to vitronectin and laminin fragment-P1
    • Aumailley, M., Gurrath, M., Muller, G., Calvete, J., Timpl, R., and Kessler, H. (1991) Arg-Gly-Asp constrained within cyclic pentapeptides-strong and selective inhibitors of cell-adhesion to vitronectin and laminin fragment-P1 FEBS Lett. 291, 50-54
    • (1991) FEBS Lett. , vol.291 , pp. 50-54
    • Aumailley, M.1    Gurrath, M.2    Muller, G.3    Calvete, J.4    Timpl, R.5    Kessler, H.6
  • 46
    • 0037186502 scopus 로고    scopus 로고
    • Nanomolar small molecule inhibitors for αvβ6, αvβ5, and αvβ3 integrins
    • Goodman, S. L., Holzemann, G., Sulyok, G. A. G., and Kessler, H. (2002) Nanomolar small molecule inhibitors for αvβ6, αvβ5, and αvβ3 integrins J. Med. Chem. 45, 1045-1051
    • (2002) J. Med. Chem. , vol.45 , pp. 1045-1051
    • Goodman, S.L.1    Holzemann, G.2    Sulyok, G.A.G.3    Kessler, H.4
  • 48
    • 79952741178 scopus 로고    scopus 로고
    • Cilengitide: The first anti-angiogenic small molecule drug candidate design, synthesis and clinical evaluation
    • Mas-Moruno, C., Rechenmacher, F., and Kessler, H. (2010) Cilengitide: the first anti-angiogenic small molecule drug candidate design, synthesis and clinical evaluation Anticancer Agents Med. Chem. 10, 753-768
    • (2010) Anticancer Agents Med. Chem. , vol.10 , pp. 753-768
    • Mas-Moruno, C.1    Rechenmacher, F.2    Kessler, H.3
  • 50
    • 84856924428 scopus 로고    scopus 로고
    • Synthesis of N-methylated cyclic peptides
    • Chatterjee, J., Laufer, B., and Kessler, H. (2012) Synthesis of N-methylated cyclic peptides Nat. Protoc. 7, 432-444
    • (2012) Nat. Protoc. , vol.7 , pp. 432-444
    • Chatterjee, J.1    Laufer, B.2    Kessler, H.3
  • 52
    • 20844455294 scopus 로고    scopus 로고
    • Convenient synthesis of N-methylamino acids compatible with Fmoc solid-phase peptide synthesis
    • Biron, E. and Kessler, H. (2005) Convenient synthesis of N-methylamino acids compatible with Fmoc solid-phase peptide synthesis J. Org. Chem. 70, 5183-5189
    • (2005) J. Org. Chem. , vol.70 , pp. 5183-5189
    • Biron, E.1    Kessler, H.2
  • 53
    • 80053645532 scopus 로고    scopus 로고
    • Venoms as a platform for human drugs: Translating toxins into therapeutics
    • King, G. F. (2011) Venoms as a platform for human drugs: translating toxins into therapeutics Expert Opin. Biol. Ther. 11, 1469-1484
    • (2011) Expert Opin. Biol. Ther. , vol.11 , pp. 1469-1484
    • King, G.F.1
  • 54
    • 0242331757 scopus 로고    scopus 로고
    • Therapeutic potential of venom peptides
    • Lewis, R. J. and Garcia, M. L. (2003) Therapeutic potential of venom peptides Nat. Rev. Drug Discovery 2, 790-802
    • (2003) Nat. Rev. Drug Discovery , vol.2 , pp. 790-802
    • Lewis, R.J.1    Garcia, M.L.2
  • 55
    • 33645028340 scopus 로고    scopus 로고
    • The cyclotides and related macrocyclic peptides as scaffolds in drug design
    • Craik, D. J., Cemazar, M., and Daly, N. L. (2006) The cyclotides and related macrocyclic peptides as scaffolds in drug design Curr. Opin. Drug Discovery Dev. 9, 251-260
    • (2006) Curr. Opin. Drug Discovery Dev. , vol.9 , pp. 251-260
    • Craik, D.J.1    Cemazar, M.2    Daly, N.L.3
  • 57
    • 80052005787 scopus 로고    scopus 로고
    • Protease-resistant peptide ligands from a knottin scaffold library
    • Getz, J. A., Rice, J. J., and Daugherty, P. S. (2011) Protease-resistant peptide ligands from a knottin scaffold library ACS Chem. Biol. 6, 837-844
    • (2011) ACS Chem. Biol. , vol.6 , pp. 837-844
    • Getz, J.A.1    Rice, J.J.2    Daugherty, P.S.3
  • 58
    • 84857048280 scopus 로고    scopus 로고
    • Cyclization of conotoxins to improve their biopharmaceutical properties
    • Clark, R. J., Akcan, M., Kaas, Q., Daly, N. L., and Craik, D. J. (2012) Cyclization of conotoxins to improve their biopharmaceutical properties Toxicon 59, 446-455
    • (2012) Toxicon , vol.59 , pp. 446-455
    • Clark, R.J.1    Akcan, M.2    Kaas, Q.3    Daly, N.L.4    Craik, D.J.5
  • 59
    • 0033529942 scopus 로고    scopus 로고
    • An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides
    • Tam, J. P., Lu, Y. A., Yang, J. L., and Chiu, K. W. (1999) An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides Proc. Natl. Acad. Sci. U.S.A. 96, 8913-8918
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 8913-8918
    • Tam, J.P.1    Lu, Y.A.2    Yang, J.L.3    Chiu, K.W.4
  • 61
    • 84864538873 scopus 로고    scopus 로고
    • Theta-defensins: Cyclic peptides with endless potential
    • Lehrer, R. I., Cole, A. M., and Selsted, M. E. (2012) Theta-defensins: cyclic peptides with endless potential J. Biol. Chem. 287, 27014-27019
    • (2012) J. Biol. Chem. , vol.287 , pp. 27014-27019
    • Lehrer, R.I.1    Cole, A.M.2    Selsted, M.E.3
  • 62
    • 84864990340 scopus 로고    scopus 로고
    • Lasso peptides: Structure, function, biosynthesis, and engineering
    • Maksimov, M. O., Pan, S. J., and Link, A. J. (2012) Lasso peptides: structure, function, biosynthesis, and engineering Nat. Prod. Rep. 29, 996-1006
    • (2012) Nat. Prod. Rep. , vol.29 , pp. 996-1006
    • Maksimov, M.O.1    Pan, S.J.2    Link, A.J.3
  • 63
    • 84861615565 scopus 로고    scopus 로고
    • Orally active peptidic bradykinin B-1 receptor antagonists engineered from a cyclotide scaffold for inflammatory pain treatment
    • Wong, C. T. T., Rowlands, D. K., Wong, C. H., Lo, T. W. C., Nguyen, G. K. T., Li, H. Y., and Tam, J. P. (2012) Orally active peptidic bradykinin B-1 receptor antagonists engineered from a cyclotide scaffold for inflammatory pain treatment Angew. Chem., Int. Ed. 51, 5620-5624
    • (2012) Angew. Chem., Int. Ed. , vol.51 , pp. 5620-5624
    • Wong, C.T.T.1    Rowlands, D.K.2    Wong, C.H.3    Lo, T.W.C.4    Nguyen, G.K.T.5    Li, H.Y.6    Tam, J.P.7
  • 65
    • 0015723952 scopus 로고
    • Effect of a polypeptide isolated from kalata-kalata (Oldenlandia-affinis DC) on estrogen dominated uterus
    • Gran, L. (1973) Effect of a polypeptide isolated from kalata-kalata (Oldenlandia-affinis DC) on estrogen dominated uterus Acta Pharmacol. Toxicol. (Copenhagen) 33, 400-408
    • (1973) Acta Pharmacol. Toxicol. (Copenhagen) , vol.33 , pp. 400-408
    • Gran, L.1
  • 66
    • 80053923631 scopus 로고    scopus 로고
    • Effects of cyclization on stability, structure, and activity of alpha-conotoxin RgIA at the alpha 9 alpha 10 nicotinic acetylcholine receptor and GABA(B) receptor
    • Halai, R., Caaghan, B., Daly, N. L., Clark, R. J., Adams, D. J., and Craik, D. J. (2011) Effects of cyclization on stability, structure, and activity of alpha-conotoxin RgIA at the alpha 9 alpha 10 nicotinic acetylcholine receptor and GABA(B) receptor J. Med. Chem. 54, 6984-6992
    • (2011) J. Med. Chem. , vol.54 , pp. 6984-6992
    • Halai, R.1    Caaghan, B.2    Daly, N.L.3    Clark, R.J.4    Adams, D.J.5    Craik, D.J.6
  • 68
    • 57549092075 scopus 로고    scopus 로고
    • Contemporary strategies for the stabilization of peptides in the alpha-helical conformation
    • Henchey, L. K., Jochim, A. L., and Arora, P. S. (2008) Contemporary strategies for the stabilization of peptides in the alpha-helical conformation Curr. Opin. Chem. Biol. 12, 692-697
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 692-697
    • Henchey, L.K.1    Jochim, A.L.2    Arora, P.S.3
  • 69
    • 84855584802 scopus 로고    scopus 로고
    • Stapled peptides for intracellular drug targets
    • (Wittrup, K. D. and Verdine, G. L. Eds.), pp, Elsevier Academic Press Inc. San Diego
    • Verdine, G. L. and Hilinski, G. J. (2012) Stapled peptides for intracellular drug targets, in Methods in Enzymology: Protein Engineering for Therapeutics, Vol 203, Pt B (Wittrup, K. D. and Verdine, G. L., Eds.), pp 3-33, Elsevier Academic Press Inc., San Diego.
    • (2012) Methods in Enzymology: Protein Engineering for Therapeutics, Vol 203, Pt B , pp. 3-33
    • Verdine, G.L.1    Hilinski, G.J.2
  • 70
    • 0023819410 scopus 로고
    • Conformational restriction of peptidyl immunogens with covalent replacements for the hydrogen bond
    • Satterthwait, A. C., Arrhenius, T., Hagopian, R. A., Zavala, F., Nussenzweig, V., and Lerner, R. A. (1988) Conformational restriction of peptidyl immunogens with covalent replacements for the hydrogen bond Vaccine 6, 99-103
    • (1988) Vaccine , vol.6 , pp. 99-103
    • Satterthwait, A.C.1    Arrhenius, T.2    Hagopian, R.A.3    Zavala, F.4    Nussenzweig, V.5    Lerner, R.A.6
  • 71
    • 0000953716 scopus 로고
    • Multicyclic polypeptide model compounds 0.2. Synthesis and conformational properties of a highly alpha-helical uncosapeptide constrained by 3 side-chain to side-chain lactam bridges
    • Osapay, G. and Taylor, J. W. (1992) Multicyclic polypeptide model compounds 0.2. Synthesis and conformational properties of a highly alpha-helical uncosapeptide constrained by 3 side-chain to side-chain lactam bridges J. Am. Chem. Soc. 114, 6966-6973
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6966-6973
    • Osapay, G.1    Taylor, J.W.2
  • 72
    • 0025007537 scopus 로고
    • Multicyclic polypeptide model compounds 0.1. Synthesis of a tricyclic amphiphilic alpha-helical peptide using an oxime resin, segment-condensation approach
    • Osapay, G. and Taylor, J. W. (1990) Multicyclic polypeptide model compounds 0.1. Synthesis of a tricyclic amphiphilic alpha-helical peptide using an oxime resin, segment-condensation approach J. Am. Chem. Soc. 112, 6046-6051
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 6046-6051
    • Osapay, G.1    Taylor, J.W.2
  • 74
    • 57549092075 scopus 로고    scopus 로고
    • Contemporary strategies for the stabilization of peptides in the α-helical conformation
    • Henchey, L. K., Jochim, A. L., and Arora, P. S. (2008) Contemporary strategies for the stabilization of peptides in the α-helical conformation Curr. Opin. Chem. Biol. 12, 692-697
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 692-697
    • Henchey, L.K.1    Jochim, A.L.2    Arora, P.S.3
  • 75
    • 0036388796 scopus 로고    scopus 로고
    • The synthesis and study of side-chain lactam-bridged peptides
    • Taylor, J. W. (2002) The synthesis and study of side-chain lactam-bridged peptides Biopolymers 66, 49-75
    • (2002) Biopolymers , vol.66 , pp. 49-75
    • Taylor, J.W.1
  • 76
    • 11944257538 scopus 로고
    • Secondary structure nucleation in peptides - Transition-metal ion stabilized alpha-helices
    • Ghadiri, M. R. and Choi, C. (1990) Secondary structure nucleation in peptides-transition-metal ion stabilized alpha-helices J. Am. Chem. Soc. 112, 1630-1632
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 1630-1632
    • Ghadiri, M.R.1    Choi, C.2
  • 77
    • 85007885646 scopus 로고
    • Iron(II) organizes a synthetic peptide into 3-helix bundles
    • Lieberman, M. and Sasaki, T. (1991) Iron(II) organizes a synthetic peptide into 3-helix bundles J. Am. Chem. Soc. 113, 1470-1471
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 1470-1471
    • Lieberman, M.1    Sasaki, T.2
  • 78
    • 80052047442 scopus 로고    scopus 로고
    • Stabilized helical peptides: Overview of the technologies and therapeutic promises
    • Estieu-Gionnet, K. and Guichard, G. (2011) Stabilized helical peptides: overview of the technologies and therapeutic promises Expert Opin. Drug Discovery 6, 937-963
    • (2011) Expert Opin. Drug Discovery , vol.6 , pp. 937-963
    • Estieu-Gionnet, K.1    Guichard, G.2
  • 80
    • 0025916569 scopus 로고
    • Cyclic parathyroid hormone-related protein antagonists: Lysine 13 to aspartic acid 17 [i to (i+ 4)] side chain to side chain lactamization
    • Chorev, M., Roubini, E., McKee, R. L., Gibbons, S. W., Goldman, M. E., Caulfield, M. P., and Rosenblatt, M. (1991) Cyclic parathyroid hormone-related protein antagonists: lysine 13 to aspartic acid 17 [i to (i+ 4)] side chain to side chain lactamization Biochemistry 30, 5968-5974
    • (1991) Biochemistry , vol.30 , pp. 5968-5974
    • Chorev, M.1    Roubini, E.2    McKee, R.L.3    Gibbons, S.W.4    Goldman, M.E.5    Caulfield, M.P.6    Rosenblatt, M.7
  • 81
    • 0030977984 scopus 로고    scopus 로고
    • Bioactivities and secondary structures of constrained analogues of human parathyroid hormone: Cyclic lactams of the receptor binding region
    • Barbier, J. R., Neugebauer, W., Morley, P., Ross, V., Soska, M., Whitfield, J. F., and Willick, G. (1997) Bioactivities and secondary structures of constrained analogues of human parathyroid hormone: Cyclic lactams of the receptor binding region J. Med. Chem. 40, 1373-1380
    • (1997) J. Med. Chem. , vol.40 , pp. 1373-1380
    • Barbier, J.R.1    Neugebauer, W.2    Morley, P.3    Ross, V.4    Soska, M.5    Whitfield, J.F.6    Willick, G.7
  • 82
    • 0035066015 scopus 로고    scopus 로고
    • The effect of monocyclic and bicyclic analogs of human parathyroid hormone (hPTH)-(1-31)NH2 on bone formation and mechanical strength in ovariectomized rats
    • Morley, P., Whitfield, J. F., Willick, G. E., Ross, V., MacLean, S., Barbier, J. R., Isaacs, R. J., and Andreassen, T. T. (2001) The effect of monocyclic and bicyclic analogs of human parathyroid hormone (hPTH)-(1-31)NH2 on bone formation and mechanical strength in ovariectomized rats Calcif. Tissue Int. 68, 95-101
    • (2001) Calcif. Tissue Int. , vol.68 , pp. 95-101
    • Morley, P.1    Whitfield, J.F.2    Willick, G.E.3    Ross, V.4    MacLean, S.5    Barbier, J.R.6    Isaacs, R.J.7    Andreassen, T.T.8
  • 83
    • 49449099743 scopus 로고    scopus 로고
    • High affinity conformationally constrained nociceptin/orphanin FQ(1-13) amide analogues
    • Charoenchai, L., Wang, H., Wang, J. B., and Aldrich, J. V. (2008) High affinity conformationally constrained nociceptin/orphanin FQ(1-13) amide analogues J. Med. Chem. 51, 4385-4387
    • (2008) J. Med. Chem. , vol.51 , pp. 4385-4387
    • Charoenchai, L.1    Wang, H.2    Wang, J.B.3    Aldrich, J.V.4
  • 84
    • 0035829411 scopus 로고    scopus 로고
    • Structure-activity studies on nociceptin analogues: ORL1 receptor binding and biological activity of cyclic disulfide-containing analogues of nociceptin peptides
    • Ambo, A., Hamazaki, N., Yamada, Y., Nakata, E., and Sasaki, Y. (2001) structure-activity studies on nociceptin analogues: ORL1 receptor binding and biological activity of cyclic disulfide-containing analogues of nociceptin peptides J. Med. Chem. 44, 4015-4018
    • (2001) J. Med. Chem. , vol.44 , pp. 4015-4018
    • Ambo, A.1    Hamazaki, N.2    Yamada, Y.3    Nakata, E.4    Sasaki, Y.5
  • 86
    • 1542721107 scopus 로고    scopus 로고
    • Cell penetrating peptides in drug delivery
    • Snyder, E. L. and Dowdy, S. F. (2004) Cell penetrating peptides in drug delivery Pharm. Res. 21, 389-393
    • (2004) Pharm. Res. , vol.21 , pp. 389-393
    • Snyder, E.L.1    Dowdy, S.F.2
  • 87
  • 88
    • 77955881153 scopus 로고    scopus 로고
    • Potent delivery of functional proteins into mammalian cells in vitro and in vivo using a supercharged protein
    • Cronican, J. J., Thompson, D. B., Beier, K. T., McNaughton, B. R., Cepko, C. L., and Liu, D. R. (2010) Potent delivery of functional proteins into mammalian cells in vitro and in vivo using a supercharged protein ACS Chem. Biol. 5, 747-752
    • (2010) ACS Chem. Biol. , vol.5 , pp. 747-752
    • Cronican, J.J.1    Thompson, D.B.2    Beier, K.T.3    McNaughton, B.R.4    Cepko, C.L.5    Liu, D.R.6
  • 89
    • 77949860245 scopus 로고    scopus 로고
    • Membrane permeable cyclic peptidyl inhibitors against human peptidylprolyl isomerase Pin1
    • Liu, T., Liu, Y., Kao, H. Y., and Pei, D. H. (2010) Membrane permeable cyclic peptidyl inhibitors against human peptidylprolyl isomerase Pin1 J. Med. Chem. 53, 2494-2501
    • (2010) J. Med. Chem. , vol.53 , pp. 2494-2501
    • Liu, T.1    Liu, Y.2    Kao, H.Y.3    Pei, D.H.4
  • 90
    • 65449148821 scopus 로고    scopus 로고
    • Mammalian cell penetration, siRNA transfection, and DNA transfection by supercharged proteins
    • McNaughton, B. R., Cronican, J. J., Thompson, D. B., and Liu, D. R. (2009) Mammalian cell penetration, siRNA transfection, and DNA transfection by supercharged proteins Proc. Natl. Acad. Sci. U.S.A. 106, 6111-6116
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 6111-6116
    • McNaughton, B.R.1    Cronican, J.J.2    Thompson, D.B.3    Liu, D.R.4
  • 91
    • 84864402585 scopus 로고    scopus 로고
    • Arginine topology controls escape of minimally cationic proteins from early endosomes to the cytoplasm
    • Appelbaum, J. S., LaRochelle, J. R., Smith, B. A., Balkin, D. M., Holub, J. M., and Schepartz, A. (2012) Arginine topology controls escape of minimally cationic proteins from early endosomes to the cytoplasm Chem. Biol. 19, 819-830
    • (2012) Chem. Biol. , vol.19 , pp. 819-830
    • Appelbaum, J.S.1    Larochelle, J.R.2    Smith, B.A.3    Balkin, D.M.4    Holub, J.M.5    Schepartz, A.6
  • 92
    • 0032542374 scopus 로고    scopus 로고
    • Highly efficient synthesis of covalently cross-linked peptide helices by ring-closing metathesis
    • Blackwell, H. E. and Grubbs, R. H. (1998) Highly efficient synthesis of covalently cross-linked peptide helices by ring-closing metathesis Angew. Chem., Int. Ed. 37, 3281-3284
    • (1998) Angew. Chem., Int. Ed. , vol.37 , pp. 3281-3284
    • Blackwell, H.E.1    Grubbs, R.H.2
  • 93
    • 0034697649 scopus 로고    scopus 로고
    • An all-hydrocarbon cross-linking system for enhancing the helicity and metabolic stability of peptides
    • Schafmeister, C. E., Po, J., and Verdine, G. L. (2000) An all-hydrocarbon cross-linking system for enhancing the helicity and metabolic stability of peptides J. Am. Chem. Soc. 122, 5891-5892
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 5891-5892
    • Schafmeister, C.E.1    Po, J.2    Verdine, G.L.3
  • 94
    • 0029860486 scopus 로고    scopus 로고
    • Application of ring-closing metathesis to the synthesis of rigidified amino acids and peptides
    • Miller, S. J., Blackwell, H. E., and Grubbs, R. H. (1996) Application of ring-closing metathesis to the synthesis of rigidified amino acids and peptides J. Am. Chem. Soc. 118, 9606-9614
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 9606-9614
    • Miller, S.J.1    Blackwell, H.E.2    Grubbs, R.H.3
  • 100
    • 77955891885 scopus 로고    scopus 로고
    • The MCL-1 BH3 helix is an exclusive MCL-1 inhibitor and apoptosis sensitizer
    • Stewart, M. L., Fire, E., Keating, A. E., and Walensky, L. D. (2010) The MCL-1 BH3 helix is an exclusive MCL-1 inhibitor and apoptosis sensitizer Nat. Chem. Biol. 6, 595-601
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 595-601
    • Stewart, M.L.1    Fire, E.2    Keating, A.E.3    Walensky, L.D.4
  • 103
    • 77449088300 scopus 로고    scopus 로고
    • Probing the alpha-helical structural stability of stapled p53 peptides: Molecular dynamics simulations and analysis
    • Guo, Z. J., Mohanty, U., Noehre, J., Sawyer, T. K., Sherman, W., and Krilov, G. (2010) Probing the alpha-helical structural stability of stapled p53 peptides: molecular dynamics simulations and analysis Chem. Biol. Drug Des. 75, 348-359
    • (2010) Chem. Biol. Drug Des. , vol.75 , pp. 348-359
    • Guo, Z.J.1    Mohanty, U.2    Noehre, J.3    Sawyer, T.K.4    Sherman, W.5    Krilov, G.6
  • 104
    • 67949084976 scopus 로고    scopus 로고
    • All-atom model for stabilization of alpha-helical structure in peptides by hydrocarbon staples
    • Kutchukian, P. S., Yang, J. S., Verdine, G. L., and Shakhnovich, E. I. (2009) All-atom model for stabilization of alpha-helical structure in peptides by hydrocarbon staples J. Am. Chem. Soc. 131, 4622-4627
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 4622-4627
    • Kutchukian, P.S.1    Yang, J.S.2    Verdine, G.L.3    Shakhnovich, E.I.4
  • 105
    • 33746052447 scopus 로고    scopus 로고
    • Evaluation of biologically relevant short α-helices stabilized by a main-chain hydrogen-bond surrogate
    • Wang, D., Chen, K., Kulp, J. L., and Arora, P. S. (2006) Evaluation of biologically relevant short α-helices stabilized by a main-chain hydrogen-bond surrogate J. Am. Chem. Soc. 128, 9248-9256
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 9248-9256
    • Wang, D.1    Chen, K.2    Kulp, J.L.3    Arora, P.S.4
  • 106
    • 4644308020 scopus 로고    scopus 로고
    • A highly stable short α-helix constrained by a main-chain hydrogen-bond surrogate
    • Chapman, R. N., Dimartino, G., and Arora, P. S. (2004) A highly stable short α-helix constrained by a main-chain hydrogen-bond surrogate J. Am. Chem. Soc. 126, 12252-12253
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 12252-12253
    • Chapman, R.N.1    Dimartino, G.2    Arora, P.S.3
  • 107
    • 65249146147 scopus 로고    scopus 로고
    • Dynamical binding of hydrogen-bond surrogate derived Bak helices to antiapoptotic protein Bcl-x L
    • Bao, J., Dong, X. Y., Zhang, J. Z. H., and Arora, P. S. (2009) Dynamical binding of hydrogen-bond surrogate derived Bak helices to antiapoptotic protein Bcl-x L J. Phys. Chem. B 113, 3565-3571
    • (2009) J. Phys. Chem. B , vol.113 , pp. 3565-3571
    • Bao, J.1    Dong, X.Y.2    Zhang, J.Z.H.3    Arora, P.S.4
  • 108
    • 41549147161 scopus 로고    scopus 로고
    • Inhibition of HIV-1 fusion by hydrogen-bond-surrogate-based alpha helices
    • Wang, D., Lu, M., and Arora, P. S. (2008) Inhibition of HIV-1 fusion by hydrogen-bond-surrogate-based alpha helices Angew. Chem., Int. Ed. 47, 1879-1882
    • (2008) Angew. Chem., Int. Ed. , vol.47 , pp. 1879-1882
    • Wang, D.1    Lu, M.2    Arora, P.S.3
  • 110
    • 79751501596 scopus 로고    scopus 로고
    • High specificity in protein recognition by hydrogen-bond-surrogate alpha-helices: Selective inhibition of the p53/MDM2 complex
    • Henchey, L. K., Porter, J. R., Ghosh, I., and Arora, P. S. (2010) High specificity in protein recognition by hydrogen-bond-surrogate alpha-helices: selective inhibition of the p53/MDM2 complex ChemBioChem 11, 2104-2107
    • (2010) ChemBioChem , vol.11 , pp. 2104-2107
    • Henchey, L.K.1    Porter, J.R.2    Ghosh, I.3    Arora, P.S.4
  • 111
    • 76149106544 scopus 로고    scopus 로고
    • Inhibition of hypoxia inducible factor 1-transcription coactivator interaction by a hydrogen bond surrogate alpha-helix
    • Henchey, L. K., Kushal, S., Dubey, R., Chapman, R. N., Olenyuk, B. Z., and Arora, P. S. (2010) Inhibition of hypoxia inducible factor 1-transcription coactivator interaction by a hydrogen bond surrogate alpha-helix J. Am. Chem. Soc. 132, 941-943
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 941-943
    • Henchey, L.K.1    Kushal, S.2    Dubey, R.3    Chapman, R.N.4    Olenyuk, B.Z.5    Arora, P.S.6
  • 113
    • 84863121468 scopus 로고    scopus 로고
    • Design of triazole-stapled BCL9 alpha-helical peptides to target the beta-catenin/B-cell CLL/lymphoma 9 (BCL9) protein-protein interaction
    • Kawamoto, S. A., Coleska, A., Ran, X., Yi, H., Yang, C. Y., and Wang, S. M. (2012) Design of triazole-stapled BCL9 alpha-helical peptides to target the beta-catenin/B-cell CLL/lymphoma 9 (BCL9) protein-protein interaction J. Med. Chem. 55, 1137-1146
    • (2012) J. Med. Chem. , vol.55 , pp. 1137-1146
    • Kawamoto, S.A.1    Coleska, A.2    Ran, X.3    Yi, H.4    Yang, C.Y.5    Wang, S.M.6
  • 114
    • 74549211258 scopus 로고    scopus 로고
    • Cu-I-catalyzed azide-alkyne intramolecular i-to-(i+4) side-chain-to-side-chain cyclization promotes the formation of helix-like secondary structures
    • Scrima, M., Le Chevalier-Isaad, A., Rovero, P., Papini, A. M., Chorev, M., and D'Ursi, A. M. (2010) Cu-I-catalyzed azide-alkyne intramolecular i-to-(i+4) side-chain-to-side-chain cyclization promotes the formation of helix-like secondary structures Eur. J. Org. Chem. 446-457
    • (2010) Eur. J. Org. Chem. , pp. 446-457
    • Scrima, M.1    Le Chevalier-Isaad, A.2    Rovero, P.3    Papini, A.M.4    Chorev, M.5    D'Ursi, A.M.6
  • 115
    • 48249146974 scopus 로고    scopus 로고
    • Synthesis and conformational analysis of a cyclic peptide obtained via i to i+4 intramolecular side-chain to side-chain azide - Alkyne 1,3-dipolar cycloaddition
    • Cantel, S., Isaad, A. L. C., Scrima, M., Levy, J. J., DiMarchi, R. D., Rovero, P., Halperin, J. A., D'Ursi, A. M., Papini, A. M., and Chorev, M. (2008) Synthesis and conformational analysis of a cyclic peptide obtained via i to i+4 intramolecular side-chain to side-chain azide-Alkyne 1,3-dipolar cycloaddition J. Org. Chem. 73, 5663-5674
    • (2008) J. Org. Chem. , vol.73 , pp. 5663-5674
    • Cantel, S.1    Isaad, A.L.C.2    Scrima, M.3    Levy, J.J.4    Dimarchi, R.D.5    Rovero, P.6    Halperin, J.A.7    D'Ursi, A.M.8    Papini, A.M.9    Chorev, M.10
  • 116
    • 79951723092 scopus 로고    scopus 로고
    • Synthesis of cell-permeable stapled peptide dual inhibitors of the p53-Mdm2/Mdmx interactions via photoinduced cycloaddition
    • Madden, M. M., Muppidi, A., Li, Z. Y., Li, X. L., Chen, J. D., and Lin, Q. (2011) Synthesis of cell-permeable stapled peptide dual inhibitors of the p53-Mdm2/Mdmx interactions via photoinduced cycloaddition Bioorg. Med. Chem. Lett. 21, 1472-1475
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 1472-1475
    • Madden, M.M.1    Muppidi, A.2    Li, Z.Y.3    Li, X.L.4    Chen, J.D.5    Lin, Q.6
  • 117
    • 70349267662 scopus 로고    scopus 로고
    • Facile synthesis of stapled, structurally reinforced peptide helices via a photoinduced intramolecular 1,3-dipolar cycloaddition reaction
    • Madden, M. M., Vera, C. I. R., Song, W. J., and Lin, Q. (2009) Facile synthesis of stapled, structurally reinforced peptide helices via a photoinduced intramolecular 1,3-dipolar cycloaddition reaction Chem. Commun. 5588-5590
    • (2009) Chem. Commun. , pp. 5588-5590
    • Madden, M.M.1    Vera, C.I.R.2    Song, W.J.3    Lin, Q.4
  • 118
    • 84863665145 scopus 로고    scopus 로고
    • Hybrid organic-inorganic inhibitors of a PDZ interaction that regulates the endocytic fate of CFTR
    • Kundu, R., Cushing, P. R., Popp, B. V., Zhao, Y., Madden, D. R., and Ball, Z. T. (2012) Hybrid organic-inorganic inhibitors of a PDZ interaction that regulates the endocytic fate of CFTR Angew. Chem., Int. Ed. 51, 7217-7220
    • (2012) Angew. Chem., Int. Ed. , vol.51 , pp. 7217-7220
    • Kundu, R.1    Cushing, P.R.2    Popp, B.V.3    Zhao, Y.4    Madden, D.R.5    Ball, Z.T.6
  • 119
    • 80053299047 scopus 로고    scopus 로고
    • A general synthesis of dirhodium metallopeptides as MDM2 ligands
    • Zaykov, A. N. and Ball, Z. T. (2011) A general synthesis of dirhodium metallopeptides as MDM2 ligands Chem. Commun. 47, 10927-10927
    • (2011) Chem. Commun. , vol.47 , pp. 10927-10927
    • Zaykov, A.N.1    Ball, Z.T.2
  • 121
    • 67650305952 scopus 로고    scopus 로고
    • Phage-encoded combinatorial chemical libraries based on bicyclic peptides
    • Heinis, C., Rutherford, T., Freund, S., and Winter, G. (2009) Phage-encoded combinatorial chemical libraries based on bicyclic peptides Nat. Chem. Biol. 5, 502-507
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 502-507
    • Heinis, C.1    Rutherford, T.2    Freund, S.3    Winter, G.4
  • 122
    • 84863485794 scopus 로고    scopus 로고
    • Peptide bicycles that inhibit the Grb2 SH2 domain
    • Quartararo, J. S., Wu, P., and Kritzer, J. A. (2012) Peptide bicycles that inhibit the Grb2 SH2 domain ChemBioChem 13, 1490-1496
    • (2012) ChemBioChem , vol.13 , pp. 1490-1496
    • Quartararo, J.S.1    Wu, P.2    Kritzer, J.A.3
  • 123
    • 0024593744 scopus 로고
    • Characterization of the human-colon carcinoma cell-line (Caco-2) as a model system for intestinal epithelial permeability
    • Hidalgo, I. J., Raub, T. J., and Borchardt, R. T. (1989) Characterization of the human-colon carcinoma cell-line (Caco-2) as a model system for intestinal epithelial permeability Gastroenterology 96, 736-749
    • (1989) Gastroenterology , vol.96 , pp. 736-749
    • Hidalgo, I.J.1    Raub, T.J.2    Borchardt, R.T.3
  • 124
    • 0031413702 scopus 로고    scopus 로고
    • Intestinal drug absorption and metabolism in cell cultures: Caco-2 and beyond
    • Artursson, P. and Borchardt, R. T. (1997) Intestinal drug absorption and metabolism in cell cultures: Caco-2 and beyond Pharm. Res. 14, 1655-1658
    • (1997) Pharm. Res. , vol.14 , pp. 1655-1658
    • Artursson, P.1    Borchardt, R.T.2
  • 125
    • 0030903756 scopus 로고    scopus 로고
    • Effect of size and charge on the passive diffusion of peptides across Caco-2 cell monolayers via the paracellular pathway
    • Pauletti, G. M., Okumu, F. W., and Borchardt, R. T. (1997) Effect of size and charge on the passive diffusion of peptides across Caco-2 cell monolayers via the paracellular pathway Pharm. Res. 14, 164-168
    • (1997) Pharm. Res. , vol.14 , pp. 164-168
    • Pauletti, G.M.1    Okumu, F.W.2    Borchardt, R.T.3
  • 126
    • 0030951009 scopus 로고    scopus 로고
    • Effect of restricted conformational flexibility on the permeation of model hexapeptides across Caco-2 cell monolayers
    • Okumu, F. W., Pauletti, G. M., VanderVelde, D. G., Siahaan, T. J., and Borchardt, R. T. (1997) Effect of restricted conformational flexibility on the permeation of model hexapeptides across Caco-2 cell monolayers Pharm. Res. 14, 169-175
    • (1997) Pharm. Res. , vol.14 , pp. 169-175
    • Okumu, F.W.1    Pauletti, G.M.2    Vandervelde, D.G.3    Siahaan, T.J.4    Borchardt, R.T.5
  • 127
    • 0030853188 scopus 로고    scopus 로고
    • The effect of beta-turn structure on the passive diffusion of peptides across Caco-2 cell monolayers
    • Knipp, G. T., Vander Velde, D. G., Siahaan, T. J., and Borchardt, R. T. (1997) The effect of beta-turn structure on the passive diffusion of peptides across Caco-2 cell monolayers Pharm. Res. 14, 1332-1340
    • (1997) Pharm. Res. , vol.14 , pp. 1332-1340
    • Knipp, G.T.1    Vander Velde, D.G.2    Siahaan, T.J.3    Borchardt, R.T.4
  • 128
    • 0030458462 scopus 로고    scopus 로고
    • How structural features influence the biomembrane permeability of peptides
    • Burton, P. S., Conradi, R. A., Ho, N. F. H., Hilgers, A. R., and Borchardt, R. T. (1996) How structural features influence the biomembrane permeability of peptides J. Pharm. Sci. 85, 1336-1340
    • (1996) J. Pharm. Sci. , vol.85 , pp. 1336-1340
    • Burton, P.S.1    Conradi, R.A.2    Ho, N.F.H.3    Hilgers, A.R.4    Borchardt, R.T.5
  • 129
    • 0027141263 scopus 로고
    • A correlation between the permeability characteristics of a series of peptides using an in vitro cell culture model (Caco-2) and those using an in situ perfused rat ileum model of the intestinal mucosa
    • Kim, D. C., Burton, P. S., and Borchardt, R. T. (1993) A correlation between the permeability characteristics of a series of peptides using an in vitro cell culture model (Caco-2) and those using an in situ perfused rat ileum model of the intestinal mucosa Pharm. Res. 10, 1710-1714
    • (1993) Pharm. Res. , vol.10 , pp. 1710-1714
    • Kim, D.C.1    Burton, P.S.2    Borchardt, R.T.3
  • 130
    • 37848999397 scopus 로고    scopus 로고
    • Effect of structural and conformation modifications, including backbone cyclization, of hydrophilic hexapeptides on their intestinal permeability and enzymatic stability
    • Hess, S., Ovadia, O., Shalev, D. E., Senderovich, H., Qadri, B., Yehezkel, T., Salitra, Y., Sheynis, T., Jelinek, R., Gilon, C., and Hoffman, A. (2007) Effect of structural and conformation modifications, including backbone cyclization, of hydrophilic hexapeptides on their intestinal permeability and enzymatic stability J. Med. Chem. 50, 6201-6211
    • (2007) J. Med. Chem. , vol.50 , pp. 6201-6211
    • Hess, S.1    Ovadia, O.2    Shalev, D.E.3    Senderovich, H.4    Qadri, B.5    Yehezkel, T.6    Salitra, Y.7    Sheynis, T.8    Jelinek, R.9    Gilon, C.10    Hoffman, A.11
  • 131
    • 0032568397 scopus 로고    scopus 로고
    • Physicochemical high throughput screening: Parallel artificial membrane permeation assay in the description of passive absorption processes
    • Kansy, M., Senner, F., and Gubernator, K. (1998) Physicochemical high throughput screening: Parallel artificial membrane permeation assay in the description of passive absorption processes J. Med. Chem. 41, 1007-1010
    • (1998) J. Med. Chem. , vol.41 , pp. 1007-1010
    • Kansy, M.1    Senner, F.2    Gubernator, K.3
  • 132
    • 0030931449 scopus 로고    scopus 로고
    • Paracellular diffusion in Caco-2 cell monolayers: Effect of perturbation on the transport of hydrophilic compounds that vary in charge and size
    • Knipp, G. T., Ho, N. F., Barsuhn, C. L., and Borchardt, R. T. (1997) Paracellular diffusion in Caco-2 cell monolayers: effect of perturbation on the transport of hydrophilic compounds that vary in charge and size J. Pharm. Sci. 86, 1105-1110
    • (1997) J. Pharm. Sci. , vol.86 , pp. 1105-1110
    • Knipp, G.T.1    Ho, N.F.2    Barsuhn, C.L.3    Borchardt, R.T.4
  • 136
    • 33644644973 scopus 로고    scopus 로고
    • Testing the conformational hypothesis of passive membrane permeability using synthetic cyclic peptide diastereomers
    • Rezai, T., Yu, B., Millhauser, G. L., Jacobson, M. P., and Lokey, R. S. (2006) Testing the conformational hypothesis of passive membrane permeability using synthetic cyclic peptide diastereomers J. Am. Chem. Soc. 128, 2510-2511
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 2510-2511
    • Rezai, T.1    Yu, B.2    Millhauser, G.L.3    Jacobson, M.P.4    Lokey, R.S.5
  • 137
    • 0034687231 scopus 로고    scopus 로고
    • Prediction of drug absorption using multivariate statistics
    • Egan, W. J., Merz, K. M., and Baldwin, J. J. (2000) Prediction of drug absorption using multivariate statistics J. Med. Chem. 43, 3867-3877
    • (2000) J. Med. Chem. , vol.43 , pp. 3867-3877
    • Egan, W.J.1    Merz, K.M.2    Baldwin, J.J.3
  • 139
    • 2342505916 scopus 로고    scopus 로고
    • Permeation of small molecules through a lipid bilayer: A computer simulation study
    • Bemporad, D., Essex, J. W., and Luttmann, C. (2004) Permeation of small molecules through a lipid bilayer: a computer simulation study J. Phys. Chem. B 108, 4875-4884
    • (2004) J. Phys. Chem. B , vol.108 , pp. 4875-4884
    • Bemporad, D.1    Essex, J.W.2    Luttmann, C.3
  • 141
    • 0030264744 scopus 로고    scopus 로고
    • Permeation process of small molecules across lipid membranes studied by molecular dynamics simulations
    • Marrink, S. J. and Berendsen, H. J. C. (1996) Permeation process of small molecules across lipid membranes studied by molecular dynamics simulations J. Phys. Chem. 100, 16729-16738
    • (1996) J. Phys. Chem. , vol.100 , pp. 16729-16738
    • Marrink, S.J.1    Berendsen, H.J.C.2
  • 144
    • 84875206151 scopus 로고
    • Trees
    • University of Chicago Press, Chicago
    • Nemerov, H. (1958) Trees, in Mirrors and Windows, University of Chicago Press, Chicago.
    • (1958) Mirrors and Windows
    • Nemerov, H.1
  • 145
    • 26844476004 scopus 로고    scopus 로고
    • Alpha-conotoxin Vc1.1 alleviates neuropathic pain and accelerates functional recovery of injured neurones
    • Satkunanathan, N., Livett, B., Gayler, K., Sandall, D., Down, J., and Khalil, Z. (2005) Alpha-conotoxin Vc1.1 alleviates neuropathic pain and accelerates functional recovery of injured neurones Brain Res. 1059, 149-158
    • (2005) Brain Res. , vol.1059 , pp. 149-158
    • Satkunanathan, N.1    Livett, B.2    Gayler, K.3    Sandall, D.4    Down, J.5    Khalil, Z.6


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