메뉴 건너뛰기




Volumn 3, Issue DEC, 2015, Pages

Recent advances toward the discovery of drug-like peptides de novo

Author keywords

Cyclic peptides; Directed evolution; Display systems; Non natural amino acids; Peptide drug discovery; Peptides and derivatives; Stability

Indexed keywords


EID: 84969506943     PISSN: None     EISSN: 22962646     Source Type: Journal    
DOI: 10.3389/fchem.2015.00069     Document Type: Short Survey
Times cited : (23)

References (77)
  • 2
    • 41949086504 scopus 로고    scopus 로고
    • Improving oral bioavailability of peptides by multiple N-methylation: somatostatin analogues
    • Biron, E., Chatterjee, J., Ovadia, O., Langenegger, D., Brueggen, J., Hoyer, D., et al. (2008). Improving oral bioavailability of peptides by multiple N-methylation: somatostatin analogues. Angew. Chem. Int. Ed. Engl. 47, 2595-2599. doi: 10.1002/anie.200705797
    • (2008) Angew. Chem. Int. Ed. Engl , vol.47 , pp. 2595-2599
    • Biron, E.1    Chatterjee, J.2    Ovadia, O.3    Langenegger, D.4    Brueggen, J.5    Hoyer, D.6
  • 3
    • 84878789554 scopus 로고    scopus 로고
    • Form and function in cyclic peptide natural products: a pharmacokinetic perspective
    • Bockus, A. T., McEwen, C. M., and Lokey, R. S. (2013). Form and function in cyclic peptide natural products: a pharmacokinetic perspective. Curr. Top. Med. Chem. 13, 821-836. doi: 10.2174/1568026611313070005
    • (2013) Curr. Top. Med. Chem , vol.13 , pp. 821-836
    • Bockus, A.T.1    McEwen, C.M.2    Lokey, R.S.3
  • 5
    • 84928700609 scopus 로고    scopus 로고
    • Dithiol amino acids can structurally shape and enhance the ligand-binding properties of polypeptides
    • Chen, S., Gopalakrishnan, R., Schaer, T., Marger, F., Hovius, R., Bertrand, D., et al. (2014). Dithiol amino acids can structurally shape and enhance the ligand-binding properties of polypeptides. Nat. Chem. 6, 1009-1016. doi: 10.1038/nchem.2043
    • (2014) Nat. Chem , vol.6 , pp. 1009-1016
    • Chen, S.1    Gopalakrishnan, R.2    Schaer, T.3    Marger, F.4    Hovius, R.5    Bertrand, D.6
  • 6
    • 33645737723 scopus 로고    scopus 로고
    • Transderml protein delivery by a coadministered peptide identified via phage display
    • Chen, Y., Shen, Y., Guo, X., Zhang, C., Yang, W., Ma, M., et al. (2006). Transderml protein delivery by a coadministered peptide identified via phage display. Nat. Biotechnol. 24, 455-460. doi: 10.1038/nbt1193
    • (2006) Nat. Biotechnol , vol.24 , pp. 455-460
    • Chen, Y.1    Shen, Y.2    Guo, X.3    Zhang, C.4    Yang, W.5    Ma, M.6
  • 7
    • 79958786544 scopus 로고    scopus 로고
    • Reprogramming the genetic code
    • Chin, J. W. (2011). Reprogramming the genetic code. EMBO J. 30, 2312-2324. doi: 10.1038/emboj.2011.160
    • (2011) EMBO J , vol.30 , pp. 2312-2324
    • Chin, J.W.1
  • 9
    • 84934996624 scopus 로고    scopus 로고
    • Hydrocarbon stapled peptides as modulators of biological function
    • Cromm, P. M., Spiegel, J., and Grossmann, T. N. (2015). Hydrocarbon stapled peptides as modulators of biological function. ACS Chem. Biol. 10, 1362-1375. doi: 10.1021/cb501020r
    • (2015) ACS Chem. Biol , vol.10 , pp. 1362-1375
    • Cromm, P.M.1    Spiegel, J.2    Grossmann, T.N.3
  • 10
    • 34548814155 scopus 로고    scopus 로고
    • Protein engineering with bacterial display
    • Daugherty, P. S. (2007). Protein engineering with bacterial display. Curr. Opin. Struct. Biol. 17, 474-480. doi: 10.1016/j.sbi.2007.07.004
    • (2007) Curr. Opin. Struct. Biol , vol.17 , pp. 474-480
    • Daugherty, P.S.1
  • 12
    • 1642524195 scopus 로고    scopus 로고
    • Identification of peptide sequences that induce the transport of phage across the gastrointestinal mucosal barrier
    • Duerr, D. M., White, S. J., and Schluesener, H. J. (2004). Identification of peptide sequences that induce the transport of phage across the gastrointestinal mucosal barrier. J. Virol. Methods 116, 177-180. doi: 10.1016/j.jviromet.2003.11.012
    • (2004) J. Virol. Methods , vol.116 , pp. 177-180
    • Duerr, D.M.1    White, S.J.2    Schluesener, H.J.3
  • 13
    • 70350442846 scopus 로고    scopus 로고
    • An in vitro selection strategy for conferring protease resistance to ligand binding peptides
    • Eldridge, B., Cooley, R. N., Odegrip, R., McGregor, D. P., Fitzgerald, K. J., and Ullman, C. G. (2009). An in vitro selection strategy for conferring protease resistance to ligand binding peptides. Protein Eng. Des. Sel. 22, 691-698. doi: 10.1093/protein/gzp052
    • (2009) Protein Eng. Des. Sel , vol.22 , pp. 691-698
    • Eldridge, B.1    Cooley, R.N.2    Odegrip, R.3    McGregor, D.P.4    Fitzgerald, K.J.5    Ullman, C.G.6
  • 14
    • 0037117459 scopus 로고    scopus 로고
    • Filamentous phage as vector-mediated antibody delivery to the brain
    • Frenkel, D., and Solomon, B. (2002). Filamentous phage as vector-mediated antibody delivery to the brain. Proc. Natl. Acad. Sci. U.S.A. 99, 5675-5679. doi: 10.1073/pnas.072027199
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 5675-5679
    • Frenkel, D.1    Solomon, B.2
  • 15
    • 84939805312 scopus 로고    scopus 로고
    • Ribosomal synthesis of macrocyclic peptides in vitro and in vivo mediated by genetically encoded aminothiol unnatural amino acids
    • Frost, J. R., Jacob, N. T., Papa, L. J., Owens, A. E., and Fasan, R. (2015). Ribosomal synthesis of macrocyclic peptides in vitro and in vivo mediated by genetically encoded aminothiol unnatural amino acids. ACS Chem. Biol. 10, 1805-1816. doi: 10.1021/acschembio.5b00119
    • (2015) ACS Chem. Biol , vol.10 , pp. 1805-1816
    • Frost, J.R.1    Jacob, N.T.2    Papa, L.J.3    Owens, A.E.4    Fasan, R.5
  • 16
    • 34648832245 scopus 로고    scopus 로고
    • Yeast surface display for protein engineering and characterization
    • Gai, S. A., and Wittrup, K. D. (2007). Yeast surface display for protein engineering and characterization. Curr. Opin. Struct. Biol. 17, 467-473. doi: 10.1016/j.sbi.2007.08.012
    • (2007) Curr. Opin. Struct. Biol , vol.17 , pp. 467-473
    • Gai, S.A.1    Wittrup, K.D.2
  • 17
    • 0036976219 scopus 로고    scopus 로고
    • A cell-penetrating peptide from a novel pVII-pIX phage-displayed random peptide library
    • Gao, C., Mao, S., Ditzel, H. J., Farnaes, L., Wirsching, P., Lerner, R. A., et al. (2002). A cell-penetrating peptide from a novel pVII-pIX phage-displayed random peptide library. Bioorg. Med. Chem. 10, 4057-4065. doi: 10.1016/S0968-0896(02)00340-1
    • (2002) Bioorg. Med. Chem , vol.10 , pp. 4057-4065
    • Gao, C.1    Mao, S.2    Ditzel, H.J.3    Farnaes, L.4    Wirsching, P.5    Lerner, R.A.6
  • 18
    • 0027404365 scopus 로고
    • Screening chemically synthesized peptide libraries for biologically-relevant molecules
    • Geysen, H. M., and Mason, T. J. (1993). Screening chemically synthesized peptide libraries for biologically-relevant molecules. Bioorg. Med. Chem. Lett. 3, 397-404. doi: 10.1016/S0960-894X(01)80221-3
    • (1993) Bioorg. Med. Chem. Lett , vol.3 , pp. 397-404
    • Geysen, H.M.1    Mason, T.J.2
  • 19
    • 84892163643 scopus 로고    scopus 로고
    • Macrocyclic drugs and clinical candidates: what can medicinal chemists learn from their properties?
    • Giordanetto, F., and Kihlberg, J. (2014). Macrocyclic drugs and clinical candidates: what can medicinal chemists learn from their properties? J. Med. Chem. 57, 278-295. doi: 10.1021/jm400887j
    • (2014) J. Med. Chem , vol.57 , pp. 278-295
    • Giordanetto, F.1    Kihlberg, J.2
  • 20
    • 77950398570 scopus 로고    scopus 로고
    • From combinatorial peptide selection to drug prototype (I): targeting the vascular endothelial growth factor receptor pathway
    • Giordano, R. J., Cardó-Vila, M., Salameh, A., Anobom, C. D., Zeitlin, B. D., Hawke, D. H., et al. (2010). From combinatorial peptide selection to drug prototype (I): targeting the vascular endothelial growth factor receptor pathway. Proc. Natl. Acad. Sci. U.S.A. 107, 5112-5117. doi: 10.1073/pnas.0915141107
    • (2010) Proc. Natl. Acad. Sci. U.S.A , vol.107 , pp. 5112-5117
    • Giordano, R.J.1    Cardó-Vila, M.2    Salameh, A.3    Anobom, C.D.4    Zeitlin, B.D.5    Hawke, D.H.6
  • 21
    • 84903151161 scopus 로고    scopus 로고
    • One-pot synthesis of azoline-containing peptides in a cell-free translation system integrated with a posttranslational cyclodehydratase
    • Goto, Y., Ito, Y., Kato, Y., Tsunoda, S., and Suga, H. (2014). One-pot synthesis of azoline-containing peptides in a cell-free translation system integrated with a posttranslational cyclodehydratase. Chem. Biol. 21, 766-774. doi: 10.1016/j.chembiol.2014.04.008
    • (2014) Chem. Biol , vol.21 , pp. 766-774
    • Goto, Y.1    Ito, Y.2    Kato, Y.3    Tsunoda, S.4    Suga, H.5
  • 22
    • 79958158209 scopus 로고    scopus 로고
    • Flexizymes for genetic code reprogramming
    • Goto, Y., Katoh, T., and Suga, H. (2011). Flexizymes for genetic code reprogramming. Nat. Protoc. 6, 779-790. doi: 10.1038/nprot.2011.331
    • (2011) Nat. Protoc , vol.6 , pp. 779-790
    • Goto, Y.1    Katoh, T.2    Suga, H.3
  • 23
    • 84861322262 scopus 로고    scopus 로고
    • Cyclotides, a novel ultrastable polypeptide scaffold for drug discovery
    • Gould, A., Ji, Y., Aboye, T. L., and Camarero, J. A. (2011). Cyclotides, a novel ultrastable polypeptide scaffold for drug discovery. Curr. Pharm. Des. 17, 4294-4307. doi: 10.2174/138161211798999438
    • (2011) Curr. Pharm. Des , vol.17 , pp. 4294-4307
    • Gould, A.1    Ji, Y.2    Aboye, T.L.3    Camarero, J.A.4
  • 24
    • 34748922922 scopus 로고    scopus 로고
    • The cyclic cystine knot miniprotein MCoTI-II is internalized into cells by macropinocytosis
    • Greenwood, K. P., Daly, N. L., Brown, D. L., Stow, J. L., and Craik, D. J. (2007). The cyclic cystine knot miniprotein MCoTI-II is internalized into cells by macropinocytosis. Int. J. Biochem. Cell Biol. 39, 2252-2264. doi: 10.1016/j.biocel.2007.06.016
    • (2007) Int. J. Biochem. Cell Biol , vol.39 , pp. 2252-2264
    • Greenwood, K.P.1    Daly, N.L.2    Brown, D.L.3    Stow, J.L.4    Craik, D.J.5
  • 25
    • 84889102141 scopus 로고    scopus 로고
    • Phage display as a technology delivering on the promise of peptide drug discovery
    • Hamzeh-Mivehroud, M., Alizadeh, A. A., Morris, M. B., Church, W. B., and Dastmalchi, S. (2013). Phage display as a technology delivering on the promise of peptide drug discovery. Drug Discov. Today 18, 1144-1157. doi: 10.1016/j.drudis.2013.09.001
    • (2013) Drug Discov. Today , vol.18 , pp. 1144-1157
    • Hamzeh-Mivehroud, M.1    Alizadeh, A.A.2    Morris, M.B.3    Church, W.B.4    Dastmalchi, S.5
  • 26
    • 0030974119 scopus 로고    scopus 로고
    • In vitro selection and evolution of functional proteins by using ribosome display
    • Hanes, J., and Plückthun, A. (1997). In vitro selection and evolution of functional proteins by using ribosome display. Proc. Natl. Acad. Sci. U.S.A. 94, 4937-4942.
    • (1997) Proc. Natl. Acad. Sci. U.S.A , vol.94 , pp. 4937-4942
    • Hanes, J.1    Plückthun, A.2
  • 27
    • 43049128964 scopus 로고    scopus 로고
    • An expanded set of amino acid analogs for the ribosomal translation of unnatural peptides
    • Hartman, M. C., Josephson, K., Lin, C. W., and Szostak, J. W. (2007). An expanded set of amino acid analogs for the ribosomal translation of unnatural peptides. PLoS ONE 2:e972. doi: 10.1371/journal.pone.0000972
    • (2007) PLoS ONE , vol.2
    • Hartman, M.C.1    Josephson, K.2    Lin, C.W.3    Szostak, J.W.4
  • 28
    • 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. doi: 10.1038/nchembio.184
    • (2009) Nat. Chem. Biol , vol.5 , pp. 502-507
    • Heinis, C.1    Rutherford, T.2    Freund, S.3    Winter, G.4
  • 29
    • 84862058523 scopus 로고    scopus 로고
    • In vitro selection of functional lantipeptides
    • Hofmann, F. T., Szostak, J. W., and Seebeck, F. P. (2012). In vitro selection of functional lantipeptides. J. Am. Chem. Soc. 134, 8038-8041. doi: 10.1021/ja302082d
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 8038-8041
    • Hofmann, F.T.1    Szostak, J.W.2    Seebeck, F.P.3
  • 30
    • 27144431943 scopus 로고    scopus 로고
    • Selecting and screening recombinant antibody libraries
    • Hoogenboom, H. R. (2005). Selecting and screening recombinant antibody libraries. Nat. Biotechnol. 23, 1105-1116. doi: 10.1038/nbt1126
    • (2005) Nat. Biotechnol , vol.23 , pp. 1105-1116
    • Hoogenboom, H.R.1
  • 31
    • 84947865948 scopus 로고    scopus 로고
    • Recombinant expression and phenotypic screening of a bioactive cyclotide against alpha-synuclein-induced cytotoxicity in baker's yeast
    • Jagadish, K., Gould, A., Borra, R., Majumder, S., Mushtaq, Z., Shekhtman, A., et al. (2015). Recombinant expression and phenotypic screening of a bioactive cyclotide against alpha-synuclein-induced cytotoxicity in baker's yeast. Angew. Chem. Int. Ed. Engl. 54, 8390-8394. doi: 10.1002/anie.201501186
    • (2015) Angew. Chem. Int. Ed. Engl , vol.54 , pp. 8390-8394
    • Jagadish, K.1    Gould, A.2    Borra, R.3    Majumder, S.4    Mushtaq, Z.5    Shekhtman, A.6
  • 32
    • 0037108767 scopus 로고    scopus 로고
    • Crystal structure of human calcineurin complexed with cyclosporin A and human cyclophilin
    • Jin, L., and Harrison, S. C. (2002). Crystal structure of human calcineurin complexed with cyclosporin A and human cyclophilin. Proc. Natl. Acad. Sci. U.S.A. 99, 13522-13526. doi: 10.1073/pnas.212504399
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 13522-13526
    • Jin, L.1    Harrison, S.C.2
  • 33
    • 84883256420 scopus 로고    scopus 로고
    • Future directions for peptide therapeutics development
    • Kaspar, A. A., and Reichert, J. M. (2013). Future directions for peptide therapeutics development. Drug Discov. Today 18, 807-817. doi: 10.1016/j.drudis.2013.05.011
    • (2013) Drug Discov. Today , vol.18 , pp. 807-817
    • Kaspar, A.A.1    Reichert, J.M.2
  • 35
    • 0025054575 scopus 로고
    • Reinvestigation of the conformation of cyclosporin A in chloroform
    • Kessler, H., Köck, M., Wein, T., and Gehrke, M. (1990). Reinvestigation of the conformation of cyclosporin A in chloroform. Helv. Chim. Acta 73, 1818-1832.
    • (1990) Helv. Chim. Acta , vol.73 , pp. 1818-1832
    • Kessler, H.1    Köck, M.2    Wein, T.3    Gehrke, M.4
  • 36
    • 84861649020 scopus 로고    scopus 로고
    • Discovery, biosynthesis, and engineering of lantipeptides
    • Knerr, P. J., and van der Donk, W. A. (2012). Discovery, biosynthesis, and engineering of lantipeptides. Annu. Rev. Biochem. 81, 479-505. doi: 10.1146/annurev-biochem-060110-113521
    • (2012) Annu. Rev. Biochem , vol.81 , pp. 479-505
    • Knerr, P.J.1    van der Donk, W.A.2
  • 37
    • 0026476589 scopus 로고
    • Conformation of cyclosporin A in polar solvents
    • Ko, S. Y., and Dalvit, C. (1992). Conformation of cyclosporin A in polar solvents. Int. J. Pept. Protein Res. 40, 380-382.
    • (1992) Int. J. Pept. Protein Res , vol.40 , pp. 380-382
    • Ko, S.Y.1    Dalvit, C.2
  • 38
    • 69249124948 scopus 로고    scopus 로고
    • Rapid selection of cyclic peptides that reduce alpha-synuclein toxicity in yeast and animal models
    • Kritzer, J. A., Hamamichi, S., McCaffery, J. M., Santagata, S., Naumann, T. A., Caldwell, K. A., et al. (2009). Rapid selection of cyclic peptides that reduce alpha-synuclein toxicity in yeast and animal models. Nat. Chem. Biol. 5, 655-663. doi: 10.1038/nchembio.193
    • (2009) Nat. Chem. Biol , vol.5 , pp. 655-663
    • Kritzer, J.A.1    Hamamichi, S.2    McCaffery, J.M.3    Santagata, S.4    Naumann, T.A.5    Caldwell, K.A.6
  • 39
    • 34447530923 scopus 로고    scopus 로고
    • Potential of phage-displayed peptide library technology to identify functional targeting peptides
    • Krumpe, L. R., and Mori, T. (2007). Potential of phage-displayed peptide library technology to identify functional targeting peptides. Expert Opin. Drug Discov. 2, 525. doi: 10.1517/17460441.2.4.525
    • (2007) Expert Opin. Drug Discov , vol.2 , pp. 525
    • Krumpe, L.R.1    Mori, T.2
  • 40
    • 0027472271 scopus 로고
    • The chemical synthesis of large random peptide libraries and their use for the discovery of ligands for macromolecular acceptors
    • Lam, K. S., Hruby, V. J., Lebl, M., Knapp, R. J., Kazmierski, W. M., Hersh, E. M., et al. (1993). The chemical synthesis of large random peptide libraries and their use for the discovery of ligands for macromolecular acceptors. Bioorg. Med. Chem. Lett. 3, 419-424. doi: 10.1016/S0960-894X(01)80224-9
    • (1993) Bioorg. Med. Chem. Lett , vol.3 , pp. 419-424
    • Lam, K.S.1    Hruby, V.J.2    Lebl, M.3    Knapp, R.J.4    Kazmierski, W.M.5    Hersh, E.M.6
  • 41
    • 33645523763 scopus 로고    scopus 로고
    • Optimizing the affinity and specificity of proteins with molecular display
    • Levin, A. M., and Weiss, G. A. (2006). Optimizing the affinity and specificity of proteins with molecular display. Mol. Biosyst. 2, 49-57. doi: 10.1039/b511782h
    • (2006) Mol. Biosyst , vol.2 , pp. 49-57
    • Levin, A.M.1    Weiss, G.A.2
  • 42
    • 0035289779 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. (2001). Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv. Drug Deliv. Rev. 46, 3-26. doi: 10.1016/S0169-409X(96)00423-1
    • (2001) Adv. Drug Deliv. Rev , vol.46 , pp. 3-26
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 45
    • 0028592703 scopus 로고
    • An in vitro polysome display system for identifying ligands from very large peptide libraries
    • Mattheakis, L. C., Bhatt, R. R., and Dower, W. J. (1994). An in vitro polysome display system for identifying ligands from very large peptide libraries. Proc. Natl. Acad. Sci. U.S.A. 91, 9022-9026.
    • (1994) Proc. Natl. Acad. Sci. U.S.A , vol.91 , pp. 9022-9026
    • Mattheakis, L.C.1    Bhatt, R.R.2    Dower, W.J.3
  • 46
    • 0027253452 scopus 로고
    • M13 bacteriophage displaying disulfide-constrained microproteins
    • McLafferty, M. A., Kent, R. B., Ladner, R. C., and Markland, W. (1993). M13 bacteriophage displaying disulfide-constrained microproteins. Gene 128, 29-36.
    • (1993) Gene , vol.128 , pp. 29-36
    • McLafferty, M.A.1    Kent, R.B.2    Ladner, R.C.3    Markland, W.4
  • 47
    • 35648992450 scopus 로고    scopus 로고
    • Design of cyclic peptides that bind protein surfaces with antibody-like affinity
    • Millward, S. W., Fiacco, S., Austin, R. J., and Roberts, R. W. (2007). Design of cyclic peptides that bind protein surfaces with antibody-like affinity. ACS Chem. Biol. 2, 625-634. doi: 10.1021/cb7001126
    • (2007) ACS Chem. Biol , vol.2 , pp. 625-634
    • Millward, S.W.1    Fiacco, S.2    Austin, R.J.3    Roberts, R.W.4
  • 48
    • 26844495780 scopus 로고    scopus 로고
    • A general route for post-translational cyclization of mRNA display libraries
    • Millward, S. W., Takahashi, T. T., and Roberts, R. W. (2005). A general route for post-translational cyclization of mRNA display libraries. J. Am. Chem. Soc. 127, 14142-14143. doi: 10.1021/ja054373h
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 14142-14143
    • Millward, S.W.1    Takahashi, T.T.2    Roberts, R.W.3
  • 49
    • 0031559943 scopus 로고    scopus 로고
    • In vitro virus: bonding of mRNA bearing puromycin at the 3'-terminal end to the C-terminal end of its encoded protein on the ribosome in vitro
    • Nemoto, N., Miyamoto-Sato, E., Husimi, Y., and Yanagawa, H. (1997). In vitro virus: bonding of mRNA bearing puromycin at the 3'-terminal end to the C-terminal end of its encoded protein on the ribosome in vitro. FEBS Lett. 414, 405-408.
    • (1997) FEBS Lett , vol.414 , pp. 405-408
    • Nemoto, N.1    Miyamoto-Sato, E.2    Husimi, Y.3    Yanagawa, H.4
  • 50
    • 84865696005 scopus 로고    scopus 로고
    • beta-Hairpin protein epitope mimetic technology in drug discovery
    • Obrecht, D., C. E., Moehle, K., and Robinson, J. (2012). beta-Hairpin protein epitope mimetic technology in drug discovery. Drug Discov. Today Technol. 9, e1-e70. doi: 10.1016/j.ddtec.2011.07.006
    • (2012) Drug Discov. Today Technol , vol.9 , pp. e1-e70
    • Obrecht, D.C.E.1    Moehle, K.2    Robinson, J.3
  • 51
    • 1542297763 scopus 로고    scopus 로고
    • CIS display: in vitro selection of peptides from libraries of protein-DNA complexes
    • Odegrip, R., Coomber, D., Eldridge, B., Hederer, R., Kuhlman, P. A., Ullman, C., et al. (2004). CIS display: in vitro selection of peptides from libraries of protein-DNA complexes. Proc. Natl. Acad. Sci. U.S.A. 101, 2806-2810. doi: 10.1073/pnas.0400219101
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 2806-2810
    • Odegrip, R.1    Coomber, D.2    Eldridge, B.3    Hederer, R.4    Kuhlman, P.A.5    Ullman, C.6
  • 52
    • 37149000703 scopus 로고    scopus 로고
    • Synthesis of polyester by means of genetic code reprogramming
    • Ohta, A., Murakami, H., Higashimura, E., and Suga, H. (2007). Synthesis of polyester by means of genetic code reprogramming. Chem. Biol. 14, 1315-1322. doi: 10.1016/j.chembiol.2007.10.015
    • (2007) Chem. Biol , vol.14 , pp. 1315-1322
    • Ohta, A.1    Murakami, H.2    Higashimura, E.3    Suga, H.4
  • 53
    • 35348892636 scopus 로고    scopus 로고
    • The flexizyme system: a highly flexible tRNA aminoacylation tool for the translation apparatus
    • Ohuchi, M., Murakami, H., and Suga, H. (2007). The flexizyme system: a highly flexible tRNA aminoacylation tool for the translation apparatus. Curr. Opin. Chem. Biol. 11, 537-542. doi: 10.1016/j.cbpa.2007.08.011
    • (2007) Curr. Opin. Chem. Biol , vol.11 , pp. 537-542
    • Ohuchi, M.1    Murakami, H.2    Suga, H.3
  • 54
    • 0026437442 scopus 로고
    • Identification of novel peptide antagonists for GPIIb/IIIa from a conformationally constrained phage peptide library
    • O'Neil, K. T., Hoess, R. H., Jackson, S. A., Ramachandran, N. S., Mousa, S. A., and DeGrado, W. F. (1992). Identification of novel peptide antagonists for GPIIb/IIIa from a conformationally constrained phage peptide library. Proteins 14, 509-515. doi: 10.1002/prot.340140411
    • (1992) Proteins , vol.14 , pp. 509-515
    • O'Neil, K.T.1    Hoess, R.H.2    Jackson, S.A.3    Ramachandran, N.S.4    Mousa, S.A.5    DeGrado, W.F.6
  • 55
    • 84987608654 scopus 로고    scopus 로고
    • Current challenges in peptide-based drug discovery
    • Otvos, L. Jr., and Wade, J. D. (2014). Current challenges in peptide-based drug discovery. Front. Chem. 2:62. doi: 10.3389/fchem.2014.00062
    • (2014) Front. Chem , vol.2 , pp. 62
    • Otvos, L.1    Wade, J.D.2
  • 56
    • 84902176344 scopus 로고    scopus 로고
    • Selection-based discovery of druglike macrocyclic peptides
    • Passioura, T., Katoh, T., Goto, Y., and Suga, H. (2014). Selection-based discovery of druglike macrocyclic peptides. Annu. Rev. Biochem. 83, 727-752. doi: 10.1146/annurev-biochem-060713-035456
    • (2014) Annu. Rev. Biochem , vol.83 , pp. 727-752
    • Passioura, T.1    Katoh, T.2    Goto, Y.3    Suga, H.4
  • 57
    • 84875686346 scopus 로고    scopus 로고
    • Selection of a high-affinity WW domain against the extracellular region of VEGF receptor isoform-2 from a combinatorial library using CIS display
    • Patel, S., Mathonet, P., Jaulent, A. M., and Ullman, C. G. (2013). Selection of a high-affinity WW domain against the extracellular region of VEGF receptor isoform-2 from a combinatorial library using CIS display. Protein Eng. Des. Sel. 26, 307-315. doi: 10.1093/protein/gzt003
    • (2013) Protein Eng. Des. Sel , vol.26 , pp. 307-315
    • Patel, S.1    Mathonet, P.2    Jaulent, A.M.3    Ullman, C.G.4
  • 58
    • 24044543111 scopus 로고    scopus 로고
    • A network of orthogonal ribosome x mRNA pairs
    • Rackham, O., and Chin, J. W. (2005). A network of orthogonal ribosome x mRNA pairs. Nat. Chem. Biol. 1, 159-166. doi: 10.1038/nchembio719
    • (2005) Nat. Chem. Biol , vol.1 , pp. 159-166
    • Rackham, O.1    Chin, J.W.2
  • 60
    • 84555196330 scopus 로고    scopus 로고
    • Charging of tRNAs using ribozymes and selection of cyclic peptides containing thioethers
    • Reid, P. C., Goto, Y., Katoh, T., and Suga, H. (2012). Charging of tRNAs using ribozymes and selection of cyclic peptides containing thioethers. Methods Mol. Biol. 805, 335-348. doi: 10.1007/978-1-61779-379-0_19
    • (2012) Methods Mol. Biol , vol.805 , pp. 335-348
    • Reid, P.C.1    Goto, Y.2    Katoh, T.3    Suga, H.4
  • 61
    • 0030817279 scopus 로고    scopus 로고
    • RNA-peptide fusions for the in vitro selection of peptides and proteins
    • Roberts, R. W., and Szostak, J. W. (1997). RNA-peptide fusions for the in vitro selection of peptides and proteins. Proc. Natl. Acad. Sci. U.S.A. 94, 12297-12302.
    • (1997) Proc. Natl. Acad. Sci. U.S.A , vol.94 , pp. 12297-12302
    • Roberts, R.W.1    Szostak, J.W.2
  • 62
    • 57049086900 scopus 로고    scopus 로고
    • Epitope mapping of antibodies using bacterial surface display
    • Rockberg, J., Löfblom, J., Hjelm, B., Uhlén, M., and Ståhl, S. (2008). Epitope mapping of antibodies using bacterial surface display. Nat. Methods 5, 1039-1045. doi: 10.1038/nmeth.1272
    • (2008) Nat. Methods , vol.5 , pp. 1039-1045
    • Rockberg, J.1    Löfblom, J.2    Hjelm, B.3    Uhlén, M.4    Ståhl, S.5
  • 63
    • 84863434152 scopus 로고    scopus 로고
    • In vitro selection of highly modified cyclic peptides that act as tight binding inhibitors
    • Schlippe, Y. V., Hartman, M. C., Josephson, K., and Szostak, J. W. (2012). In vitro selection of highly modified cyclic peptides that act as tight binding inhibitors. J. Am. Chem. Soc. 134, 10469-10477. doi: 10.1021/ja301017y
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 10469-10477
    • Schlippe, Y.V.1    Hartman, M.C.2    Josephson, K.3    Szostak, J.W.4
  • 64
    • 79956079627 scopus 로고    scopus 로고
    • Artificial lantipeptides from in vitro translations
    • Seebeck, F. P., Ricardo, A., and Szostak, J. W. (2011). Artificial lantipeptides from in vitro translations. Chem. Commun. 47, 6141-6143. doi: 10.1039/c0cc05663d
    • (2011) Chem. Commun , vol.47 , pp. 6141-6143
    • Seebeck, F.P.1    Ricardo, A.2    Szostak, J.W.3
  • 65
    • 33751540859 scopus 로고    scopus 로고
    • Display technologies: application for the discovery of drug and gene delivery agents
    • Sergeeva, A., Kolonin, M. G., Molldrem, J. J., Pasqualini, R., and Arap, W. (2006). Display technologies: application for the discovery of drug and gene delivery agents. Adv. Drug Deliv. Rev. 58, 1622-1654. doi: 10.1016/j.addr.2006.09.018
    • (2006) Adv. Drug Deliv. Rev , vol.58 , pp. 1622-1654
    • Sergeeva, A.1    Kolonin, M.G.2    Molldrem, J.J.3    Pasqualini, R.4    Arap, W.5
  • 67
    • 23044504786 scopus 로고    scopus 로고
    • Protein synthesis by pure translation systems
    • Shimizu, Y., Kanamori, T., and Ueda, T. (2005). Protein synthesis by pure translation systems. Methods 36, 299-304. doi: 10.1016/j.ymeth.2005.04.006
    • (2005) Methods , vol.36 , pp. 299-304
    • Shimizu, Y.1    Kanamori, T.2    Ueda, T.3
  • 69
  • 70
    • 43249113921 scopus 로고    scopus 로고
    • Ribosomal synthesis of N-methyl peptides
    • Subtelny, A. O., Hartman, M. C., and Szostak, J. W. (2008). Ribosomal synthesis of N-methyl peptides. J. Am. Chem. Soc. 130, 6131-6136. doi: 10.1021/ja710016v
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 6131-6136
    • Subtelny, A.O.1    Hartman, M.C.2    Szostak, J.W.3
  • 71
    • 79953004613 scopus 로고    scopus 로고
    • Optimal codon choice can improve the efficiency and fidelity of N-methyl amino acid incorporation into peptides by in-vitro translation
    • Subtelny, A. O., Hartman, M. C., and Szostak, J. W. (2011). Optimal codon choice can improve the efficiency and fidelity of N-methyl amino acid incorporation into peptides by in-vitro translation. Angew. Chem. Int. Ed. Engl. 50, 3164-3167. doi: 10.1002/anie.201007686
    • (2011) Angew. Chem. Int. Ed. Engl , vol.50 , pp. 3164-3167
    • Subtelny, A.O.1    Hartman, M.C.2    Szostak, J.W.3
  • 72
    • 80054780096 scopus 로고    scopus 로고
    • In vitro methods for peptide display and their applications
    • Ullman, C. G., Frigotto, L., and Cooley, R. N. (2011). In vitro methods for peptide display and their applications. Brief. Funct. Genomics 10, 125-134. doi: 10.1093/bfgp/elr010
    • (2011) Brief. Funct. Genomics , vol.10 , pp. 125-134
    • Ullman, C.G.1    Frigotto, L.2    Cooley, R.N.3
  • 73
    • 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. doi: 10.1021/jm020017n
    • (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
  • 74
    • 84929084835 scopus 로고    scopus 로고
    • Exploring experimental and computational markers of cyclic peptides: charting islands of permeability
    • Wang, C. K., Northfield, S. E., Swedberg, J. E., Colless, B., Chaousis, S., Price, D. A., et al. (2015). Exploring experimental and computational markers of cyclic peptides: charting islands of permeability. Eur. J. Med. Chem. 97, 202-213. doi: 10.1016/j.ejmech.2015.04.049
    • (2015) Eur. J. Med. Chem , vol.97 , pp. 202-213
    • Wang, C.K.1    Northfield, S.E.2    Swedberg, J.E.3    Colless, B.4    Chaousis, S.5    Price, D.A.6
  • 75
    • 80054853098 scopus 로고    scopus 로고
    • On-resin N-methylation of cyclic peptides for discovery of orally bioavailable scaffolds
    • White, T. R., Renzelman, C. M., Rand, A. C., Rezai, T., McEwen, C. M., Gelev, V. M., et al. (2011). On-resin N-methylation of cyclic peptides for discovery of orally bioavailable scaffolds. Nat. Chem. Biol. 7, 810-817. doi: 10.1038/nchembio.664
    • (2011) Nat. Chem. Biol , vol.7 , pp. 810-817
    • White, T.R.1    Renzelman, C.M.2    Rand, A.C.3    Rezai, T.4    McEwen, C.M.5    Gelev, V.M.6
  • 77
    • 47549110353 scopus 로고    scopus 로고
    • Structural basis of specific tRNA aminoacylation by a small in vitro selected ribozyme
    • Xiao, H., Murakami, H., Suga, H., and Ferré-D'Amaré, A. R. (2008). Structural basis of specific tRNA aminoacylation by a small in vitro selected ribozyme. Nature 454, 358-361. doi: 10.1038/nature07033
    • (2008) Nature , vol.454 , pp. 358-361
    • Xiao, H.1    Murakami, H.2    Suga, H.3    Ferré-D'Amaré, A.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.