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Volumn 38, Issue , 2017, Pages 52-61

Exploring sequence space: harnessing chemical and biological diversity towards new peptide leads

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; MESSENGER RNA; PEPTIDE DERIVATIVE; PEPTIDE;

EID: 85015408648     PISSN: 13675931     EISSN: 18790402     Source Type: Journal    
DOI: 10.1016/j.cbpa.2017.02.020     Document Type: Review
Times cited : (66)

References (69)
  • 1
    • 84871365798 scopus 로고    scopus 로고
    • Expanding the number of “druggable targets”: non-enzymes and protein–protein interactions
    • 1 Makley, L.N., Gestwicki, J.E., Expanding the number of “druggable targets”: non-enzymes and protein–protein interactions. Chem Biol Drug Des 81 (2013), 22–32.
    • (2013) Chem Biol Drug Des , vol.81 , pp. 22-32
    • Makley, L.N.1    Gestwicki, J.E.2
  • 2
    • 84930015010 scopus 로고    scopus 로고
    • Peptide therapeutics: targeting the undruggable space
    • 2 Tsomaia, N., Peptide therapeutics: targeting the undruggable space. Eur J Med Chem 94 (2015), 459–470.
    • (2015) Eur J Med Chem , vol.94 , pp. 459-470
    • Tsomaia, N.1
  • 4
    • 84924705949 scopus 로고    scopus 로고
    • Encoded libraries of chemically modified peptides
    • 4 Heinis, C., Winter, G., Encoded libraries of chemically modified peptides. Curr Opin Chem Biol 26 (2015), 89–98.
    • (2015) Curr Opin Chem Biol , vol.26 , pp. 89-98
    • Heinis, C.1    Winter, G.2
  • 5
    • 0026419328 scopus 로고
    • A new type of synthetic peptide library for identifying ligand-binding activity
    • 5 Lam, K.S., Salmon, S.E., Hersh, E.M., Hruby, V.J., Kazmierski, W.M., Knapp, R.J., A new type of synthetic peptide library for identifying ligand-binding activity. Nature 354 (1991), 82–84.
    • (1991) Nature , vol.354 , pp. 82-84
    • Lam, K.S.1    Salmon, S.E.2    Hersh, E.M.3    Hruby, V.J.4    Kazmierski, W.M.5    Knapp, R.J.6
  • 6
    • 74249109746 scopus 로고    scopus 로고
    • De novo sequencing of peptides on single resin beads by MALDI-FTICR tandem mass spectrometry
    • 6 Semmler, A., Weber, R., Przybylski, M., Wittmann, V., De novo sequencing of peptides on single resin beads by MALDI-FTICR tandem mass spectrometry. J Am Soc Mass Spectrom 21 (2010), 215–219.
    • (2010) J Am Soc Mass Spectrom , vol.21 , pp. 215-219
    • Semmler, A.1    Weber, R.2    Przybylski, M.3    Wittmann, V.4
  • 7
    • 84922041528 scopus 로고    scopus 로고
    • Synthesis and screening of one-bead-one-compound cyclic peptide libraries
    • R. Derda Springer New York
    • 7 Qian, Z., Upadhyaya, P., Pei, D., Synthesis and screening of one-bead-one-compound cyclic peptide libraries. Derda, R., (eds.) Peptide Libraries: Methods and Protocols, 2015, Springer, New York, 39–53.
    • (2015) Peptide Libraries: Methods and Protocols , pp. 39-53
    • Qian, Z.1    Upadhyaya, P.2    Pei, D.3
  • 8
    • 84969506943 scopus 로고    scopus 로고
    • Recent advances toward the discovery of drug-like peptides de novo
    • 8 Goldflam, M., Ullman, C.G., Recent advances toward the discovery of drug-like peptides de novo. Front Chem, 3, 2015, 69.
    • (2015) Front Chem , vol.3 , pp. 69
    • Goldflam, M.1    Ullman, C.G.2
  • 10
    • 84906060855 scopus 로고    scopus 로고
    • Peptides come round: using SICLOPPS libraries for early stage drug discovery
    • 10 Lennard, K.R., Tavassoli, A., Peptides come round: using SICLOPPS libraries for early stage drug discovery. Chemistry 20 (2014), 10608–10614.
    • (2014) Chemistry , vol.20 , pp. 10608-10614
    • Lennard, K.R.1    Tavassoli, A.2
  • 13
    • 34447530923 scopus 로고    scopus 로고
    • Potential of phage-displayed peptide library technology to identify functional targeting peptides
    • 13 Krumpe, L., Mori, T., Potential of phage-displayed peptide library technology to identify functional targeting peptides. Expert Opin Drug Discov, 2, 2007, 525.
    • (2007) Expert Opin Drug Discov , vol.2 , pp. 525
    • Krumpe, L.1    Mori, T.2
  • 14
  • 15
    • 0347359106 scopus 로고    scopus 로고
    • Phosphotyrosine phosphoepitopes can be rapidly analyzed by coexpression of a tyrosine kinase in bacteria with a T7 bacteriophage display library
    • 15 Khati, M., Pillay, T.S., Phosphotyrosine phosphoepitopes can be rapidly analyzed by coexpression of a tyrosine kinase in bacteria with a T7 bacteriophage display library. Anal Biochem 325 (2004), 164–167.
    • (2004) Anal Biochem , vol.325 , pp. 164-167
    • Khati, M.1    Pillay, T.S.2
  • 16
    • 0030817279 scopus 로고    scopus 로고
    • RNA–peptide fusions for the in vitro selection of peptides and proteins
    • 16 Roberts, R.W., Szostak, J.W., RNA–peptide fusions for the in vitro selection of peptides and proteins. Proc Natl Acad Sci U S A 94 (1997), 12297–12302.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 12297-12302
    • Roberts, R.W.1    Szostak, J.W.2
  • 17
    • 84940845423 scopus 로고    scopus 로고
    • Discovering functional, non-proteinogenic amino acid containing, peptides using genetic code reprogramming
    • 17 Rogers, J.M., Suga, H., Discovering functional, non-proteinogenic amino acid containing, peptides using genetic code reprogramming. Org Biomol Chem 13 (2015), 9353–9363.
    • (2015) Org Biomol Chem , vol.13 , pp. 9353-9363
    • Rogers, J.M.1    Suga, H.2
  • 18
    • 85003550710 scopus 로고    scopus 로고
    • Improving the binding affinity of in-vitro-evolved cyclic peptides by inserting atoms into the macrocycle backbone
    • 18 Wilbs, J., Middendorp, S.J., Heinis, C., Improving the binding affinity of in-vitro-evolved cyclic peptides by inserting atoms into the macrocycle backbone. ChemBioChem 17 (2016), 2299–2303.
    • (2016) ChemBioChem , vol.17 , pp. 2299-2303
    • Wilbs, J.1    Middendorp, S.J.2    Heinis, C.3
  • 19
    • 84863434152 scopus 로고    scopus 로고
    • In vitro selection of highly modified cyclic peptides that act as tight binding inhibitors
    • 19 Guillen Schlippe, Y.V., Hartman, M.C.T., Josephson, K., Szostak, J.W., In vitro selection of highly modified cyclic peptides that act as tight binding inhibitors. J Am Chem Soc 134 (2012), 10469–10477.
    • (2012) J Am Chem Soc , vol.134 , pp. 10469-10477
    • Guillen Schlippe, Y.V.1    Hartman, M.C.T.2    Josephson, K.3    Szostak, J.W.4
  • 20
    • 58049219079 scopus 로고    scopus 로고
    • Ribosomal synthesis of polypeptoids and peptoid–peptide hybrids
    • 20 Kawakami, T., Murakami, H., Suga, H., Ribosomal synthesis of polypeptoids and peptoid–peptide hybrids. J Am Chem Soc 130 (2008), 16861–16863.
    • (2008) J Am Chem Soc , vol.130 , pp. 16861-16863
    • Kawakami, T.1    Murakami, H.2    Suga, H.3
  • 21
    • 84883077144 scopus 로고    scopus 로고
    • Extensive reprogramming of the genetic code for genetically encoded synthesis of highly N-alkylated polycyclic peptidomimetics
    • 21 Kawakami, T., Ishizawa, T., Murakami, H., Extensive reprogramming of the genetic code for genetically encoded synthesis of highly N-alkylated polycyclic peptidomimetics. J Am Chem Soc 135 (2013), 12297–12304.
    • (2013) J Am Chem Soc , vol.135 , pp. 12297-12304
    • Kawakami, T.1    Ishizawa, T.2    Murakami, H.3
  • 22
    • 0018265171 scopus 로고
    • “Chemical aminoacylation” of tRNA's
    • 22 Hecht, S.M., Alford, B.L., Kuroda, Y., Kitano, S., “Chemical aminoacylation” of tRNA's. J Biol Chem 253 (1978), 4517–4520.
    • (1978) J Biol Chem , vol.253 , pp. 4517-4520
    • Hecht, S.M.1    Alford, B.L.2    Kuroda, Y.3    Kitano, S.4
  • 23
    • 77951236321 scopus 로고    scopus 로고
    • Beyond the canonical 20 amino acids: expanding the genetic lexicon
    • 23 Young, T.S., Schultz, P.G., Beyond the canonical 20 amino acids: expanding the genetic lexicon. J Biol Chem 285 (2010), 11039–11044.
    • (2010) J Biol Chem , vol.285 , pp. 11039-11044
    • Young, T.S.1    Schultz, P.G.2
  • 24
    • 84255189091 scopus 로고    scopus 로고
    • Flexizymes: their evolutionary history and the origin of catalytic function
    • 24 Morimoto, J., Hayashi, Y., Iwasaki, K., Suga, H., Flexizymes: their evolutionary history and the origin of catalytic function. Acc Chem Res 44 (2011), 1359–1368.
    • (2011) Acc Chem Res , vol.44 , pp. 1359-1368
    • Morimoto, J.1    Hayashi, Y.2    Iwasaki, K.3    Suga, H.4
  • 25
    • 84961674028 scopus 로고    scopus 로고
    • Expanding the amino acid repertoire of ribosomal polypeptide synthesis via the artificial division of codon boxes
    • Through construction of a PURE-based artificial translation system with all native ARSs omitted the authors demonstrate the potential to significantly expand the genetic code by introduction of all desired pre-amino-acylated tRNAs.
    • 25•• Iwane, Y., Hitomi, A., Murakami, H., Katoh, T., Goto, Y., Suga, H., Expanding the amino acid repertoire of ribosomal polypeptide synthesis via the artificial division of codon boxes. Nat Chem 8 (2016), 317–325 Through construction of a PURE-based artificial translation system with all native ARSs omitted the authors demonstrate the potential to significantly expand the genetic code by introduction of all desired pre-amino-acylated tRNAs.
    • (2016) Nat Chem , vol.8 , pp. 317-325
    • Iwane, Y.1    Hitomi, A.2    Murakami, H.3    Katoh, T.4    Goto, Y.5    Suga, H.6
  • 26
    • 84977103522 scopus 로고    scopus 로고
    • Genetic code expansion by degeneracy reprogramming of arginyl codons
    • The authors artificially divide the arginine codon box by removal of native arginine tRNAs using Colicin D and reintroduction of individually pre-charged arginine tRNAs.
    • 26• Lee, K.B., Hou, C.Y., Kim, C.E., Kim, D.M., Suga, H., Kang, T.J., Genetic code expansion by degeneracy reprogramming of arginyl codons. ChemBioChem 17 (2016), 1198–1201 The authors artificially divide the arginine codon box by removal of native arginine tRNAs using Colicin D and reintroduction of individually pre-charged arginine tRNAs.
    • (2016) ChemBioChem , vol.17 , pp. 1198-1201
    • Lee, K.B.1    Hou, C.Y.2    Kim, C.E.3    Kim, D.M.4    Suga, H.5    Kang, T.J.6
  • 27
    • 84859627442 scopus 로고    scopus 로고
    • Ribosomal production and in vitro selection of natural product-like peptidomimetics: the FIT and RaPID systems
    • 27 Hipolito, C.J., Suga, H., Ribosomal production and in vitro selection of natural product-like peptidomimetics: the FIT and RaPID systems. Curr Opin Chem Biol 16 (2012), 196–203.
    • (2012) Curr Opin Chem Biol , vol.16 , pp. 196-203
    • Hipolito, C.J.1    Suga, H.2
  • 28
    • 84959019914 scopus 로고    scopus 로고
    • Ribosomal synthesis of peptides with multiple β-amino acids
    • The authors singly introduce 13 different β-amino acids into a peptide chain, providing the first example of such wildtype ribosomal incorporation.
    • 28•• Fujino, T., Goto, Y., Suga, H., Murakami, H., Ribosomal synthesis of peptides with multiple β-amino acids. J Am Chem Soc 138 (2016), 1962–1969 The authors singly introduce 13 different β-amino acids into a peptide chain, providing the first example of such wildtype ribosomal incorporation.
    • (2016) J Am Chem Soc , vol.138 , pp. 1962-1969
    • Fujino, T.1    Goto, Y.2    Suga, H.3    Murakami, H.4
  • 29
    • 84873389412 scopus 로고    scopus 로고
    • Reevaluation of the D-amino acid compatibility with the elongation event in translation
    • 29 Fujino, T., Goto, Y., Suga, H., Murakami, H., Reevaluation of the D-amino acid compatibility with the elongation event in translation. J Am Chem Soc 135 (2013), 1830–1837.
    • (2013) J Am Chem Soc , vol.135 , pp. 1830-1837
    • Fujino, T.1    Goto, Y.2    Suga, H.3    Murakami, H.4
  • 30
    • 38349027623 scopus 로고    scopus 로고
    • Reprogramming the translation initiation for the synthesis of physiologically stable cyclic peptides
    • 30 Goto, Y., Ohta, A., Sako, Y., Yamagishi, Y., Murakami, H., Suga, H., Reprogramming the translation initiation for the synthesis of physiologically stable cyclic peptides. ACS Chem Biol 3 (2008), 120–129.
    • (2008) ACS Chem Biol , vol.3 , pp. 120-129
    • Goto, Y.1    Ohta, A.2    Sako, Y.3    Yamagishi, Y.4    Murakami, H.5    Suga, H.6
  • 33
    • 38349062552 scopus 로고    scopus 로고
    • Messenger RNA-programmed incorporation of multiple N-methyl-amino acids into linear and cyclic peptides
    • 33 Kawakami, T., Murakami, H., Suga, H., Messenger RNA-programmed incorporation of multiple N-methyl-amino acids into linear and cyclic peptides. Chem Biol 15 (2008), 32–42.
    • (2008) Chem Biol , vol.15 , pp. 32-42
    • Kawakami, T.1    Murakami, H.2    Suga, H.3
  • 34
    • 45749150319 scopus 로고    scopus 로고
    • Initiating translation with D-amino acids
    • 34 Goto, Y., Murakami, H., Suga, H., Initiating translation with D-amino acids. RNA 14 (2008), 1390–1398.
    • (2008) RNA , vol.14 , pp. 1390-1398
    • Goto, Y.1    Murakami, H.2    Suga, H.3
  • 36
    • 85009431697 scopus 로고    scopus 로고
    • Consecutive elongation of D-amino acids in translation
    • Glu and translation system (increased EF-Tu/Ts, IF2 and decreased EF-G).
    • Glu and translation system (increased EF-Tu/Ts, IF2 and decreased EF-G).
    • (2017) Cell Chem Biol , vol.24 , pp. 46-54
    • Katoh, T.1    Tajima, K.2    Suga, H.3
  • 37
    • 84943541737 scopus 로고    scopus 로고
    • Post-translational introduction of D-alanine into ribosomally synthesized peptides by the dehydroalanine reductase NpnJ
    • The authors show the assymetric reduction of dehydroalanine, generated from serine, using NpnJ reductase and NADPH. Their reconstituted in vitro system shows a broad substrate tolerance.
    • 37• Yang, X., Van Der Donk, W.A., Post-translational introduction of D-alanine into ribosomally synthesized peptides by the dehydroalanine reductase NpnJ. J Am Chem Soc 137 (2015), 12426–12429 The authors show the assymetric reduction of dehydroalanine, generated from serine, using NpnJ reductase and NADPH. Their reconstituted in vitro system shows a broad substrate tolerance.
    • (2015) J Am Chem Soc , vol.137 , pp. 12426-12429
    • Yang, X.1    Van Der Donk, W.A.2
  • 38
    • 85016293162 scopus 로고    scopus 로고
    • Seven enzymes create extraordinary molecular complexity in an uncultivated bacterium
    • Polytheonamide is a ribosomal peptide, with up to 50 site specific post-translational modifications including epimerization and methylation. Here, the authors show that only seven enzymes are sufficient for generating the final peptide.
    • 38• Freeman, M.F., Helf, M.J., Bhushan, A., Morinaka, B.I., Piel, J., Seven enzymes create extraordinary molecular complexity in an uncultivated bacterium. Nat Chem, 2016, 10.1038/NCHEM.2666 Polytheonamide is a ribosomal peptide, with up to 50 site specific post-translational modifications including epimerization and methylation. Here, the authors show that only seven enzymes are sufficient for generating the final peptide.
    • (2016) Nat Chem
    • Freeman, M.F.1    Helf, M.J.2    Bhushan, A.3    Morinaka, B.I.4    Piel, J.5
  • 39
    • 84903151161 scopus 로고    scopus 로고
    • One-pot synthesis of azoline-containing peptides in a cell-free translation system integrated with a posttranslational cyclodehydratase
    • The authors have established a one-pot procedure for generating azoline containing peptidesin vitro by combining the FIT system with the posttranslational cyclodehydratase PatD.
    • 39• Goto, Y., Ito, Y., Kato, Y., Tsunoda, S., Suga, H., One-pot synthesis of azoline-containing peptides in a cell-free translation system integrated with a posttranslational cyclodehydratase. Chem Biol 21 (2014), 766–774 The authors have established a one-pot procedure for generating azoline containing peptidesin vitro by combining the FIT system with the posttranslational cyclodehydratase PatD.
    • (2014) Chem Biol , vol.21 , pp. 766-774
    • Goto, Y.1    Ito, Y.2    Kato, Y.3    Tsunoda, S.4    Suga, H.5
  • 40
    • 84994026531 scopus 로고    scopus 로고
    • A post-translational cyclodehydratase, PatD, tolerates sequence variation in the C-terminal region of substrate peptides
    • 40 Goto, Y., Suga, H., A post-translational cyclodehydratase, PatD, tolerates sequence variation in the C-terminal region of substrate peptides. Chem Lett 45 (2016), 1247–1249.
    • (2016) Chem Lett , vol.45 , pp. 1247-1249
    • Goto, Y.1    Suga, H.2
  • 41
    • 84902244730 scopus 로고    scopus 로고
    • Rapid, hydrolytically stable modification of aldehyde-terminated proteins and phage libraries
    • 41 Kitov, P.I., Vinals, D.F., Ng, S., Tjhung, K.F., Derda, R., Rapid, hydrolytically stable modification of aldehyde-terminated proteins and phage libraries. J Am Chem Soc 136 (2014), 8149–8152.
    • (2014) J Am Chem Soc , vol.136 , pp. 8149-8152
    • Kitov, P.I.1    Vinals, D.F.2    Ng, S.3    Tjhung, K.F.4    Derda, R.5
  • 42
    • 84954443573 scopus 로고    scopus 로고
    • Silent encoding of chemical post-translational modifications in phage-displayed libraries
    • 42 Tjhung, K.F., Kitov, P.I., Ng, S., Kitova, E.N., Deng, L., Klassen, J.S., Derda, R., Silent encoding of chemical post-translational modifications in phage-displayed libraries. J Am Chem Soc 138 (2016), 32–35.
    • (2016) J Am Chem Soc , vol.138 , pp. 32-35
    • Tjhung, K.F.1    Kitov, P.I.2    Ng, S.3    Kitova, E.N.4    Deng, L.5    Klassen, J.S.6    Derda, R.7
  • 43
    • 84881369201 scopus 로고    scopus 로고
    • A monosaccharide-modified peptide phage library for screening of ligands to carbohydrate-binding proteins
    • 43 Arai, K., Tsutsumi, H., Mihara, H., A monosaccharide-modified peptide phage library for screening of ligands to carbohydrate-binding proteins. Bioorg Med Chem Lett 23 (2013), 4940–4943.
    • (2013) Bioorg Med Chem Lett , vol.23 , pp. 4940-4943
    • Arai, K.1    Tsutsumi, H.2    Mihara, H.3
  • 44
    • 0037348840 scopus 로고    scopus 로고
    • A novel strategy for in vitro selection of peptide–drug conjugates
    • 44 Li, S., Roberts, R.W., A novel strategy for in vitro selection of peptide–drug conjugates. Chem Biol 10 (2003), 233–239.
    • (2003) Chem Biol , vol.10 , pp. 233-239
    • Li, S.1    Roberts, R.W.2
  • 46
    • 67650305952 scopus 로고    scopus 로고
    • Phage-encoded combinatorial chemical libraries based on bicyclic peptides
    • 46 Heinis, C., Rutherford, T., Freund, S., Winter, G., Phage-encoded combinatorial chemical libraries based on bicyclic peptides. Nat Chem Biol 5 (2009), 502–507.
    • (2009) Nat Chem Biol , vol.5 , pp. 502-507
    • Heinis, C.1    Rutherford, T.2    Freund, S.3    Winter, G.4
  • 47
    • 21044441799 scopus 로고    scopus 로고
    • Rapid and quantitative cyclization of multiple peptide loops onto synthetic scaffolds for structural mimicry of protein surfaces
    • 47 Timmerman, P., Beld, J., Puijk, W.C., Meloen, R.H., Rapid and quantitative cyclization of multiple peptide loops onto synthetic scaffolds for structural mimicry of protein surfaces. ChemBioChem 6 (2005), 821–824.
    • (2005) ChemBioChem , vol.6 , pp. 821-824
    • Timmerman, P.1    Beld, J.2    Puijk, W.C.3    Meloen, R.H.4
  • 49
    • 84935007768 scopus 로고    scopus 로고
    • Synthesis of fused tricyclic peptides using a reprogrammed translation system and chemical modification
    • 49 Bashiruddin, N.K., Nagano, M., Suga, H., Synthesis of fused tricyclic peptides using a reprogrammed translation system and chemical modification. Bioorg Chem 61 (2015), 45–50.
    • (2015) Bioorg Chem , vol.61 , pp. 45-50
    • Bashiruddin, N.K.1    Nagano, M.2    Suga, H.3
  • 50
    • 82955227984 scopus 로고    scopus 로고
    • Bacterial display and screening of posttranslationally thioether-stabilized peptides
    • 50 Bosma, T., Kuipers, A., Bulten, E., de Vries, L., Rink, R., Moll, G.N., Bacterial display and screening of posttranslationally thioether-stabilized peptides. Appl Environ Microbiol 77 (2011), 6794–6801.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 6794-6801
    • Bosma, T.1    Kuipers, A.2    Bulten, E.3    de Vries, L.4    Rink, R.5    Moll, G.N.6
  • 51
    • 70349556387 scopus 로고    scopus 로고
    • Ribosomal synthesis of cyclic peptides with a fluorogenic oxidative coupling reaction
    • 51 Yamagishi, Y., Ashigai, H., Goto, Y., Murakami, H., Suga, H., Ribosomal synthesis of cyclic peptides with a fluorogenic oxidative coupling reaction. ChemBioChem 10 (2009), 1469–1472.
    • (2009) ChemBioChem , vol.10 , pp. 1469-1472
    • Yamagishi, Y.1    Ashigai, H.2    Goto, Y.3    Murakami, H.4    Suga, H.5
  • 52
    • 44949231370 scopus 로고    scopus 로고
    • Ribosomal synthesis of bicyclic peptides via two orthogonal inter-side-chain reactions
    • 52 Sako, Y., Morimoto, J., Murakami, H., Suga, H., Ribosomal synthesis of bicyclic peptides via two orthogonal inter-side-chain reactions. J Am Chem Soc 130 (2008), 7232–7234.
    • (2008) J Am Chem Soc , vol.130 , pp. 7232-7234
    • Sako, Y.1    Morimoto, J.2    Murakami, H.3    Suga, H.4
  • 55
    • 84995793657 scopus 로고    scopus 로고
    • Allosteric inhibition of a Semaphorin 4D receptor Plexin B1 by a high-affinity macrocyclic peptide
    • The authors show the generation and characterisation of a macrocyclic peptide, which allosterically inhibits Semaphorin receptor Plexin B1.
    • 55• Matsunaga, Y., Bashiruddin, N.K., Kitago, Y., Takagi, J., Suga, H., Allosteric inhibition of a Semaphorin 4D receptor Plexin B1 by a high-affinity macrocyclic peptide. Cell Chem Biol 23 (2016), 1341–1350 The authors show the generation and characterisation of a macrocyclic peptide, which allosterically inhibits Semaphorin receptor Plexin B1.
    • (2016) Cell Chem Biol , vol.23 , pp. 1341-1350
    • Matsunaga, Y.1    Bashiruddin, N.K.2    Kitago, Y.3    Takagi, J.4    Suga, H.5
  • 56
    • 85014117670 scopus 로고    scopus 로고
    • Rapid discovery of potent and selective glycosidase-inhibiting de novo peptides
    • The authors use the RaPID system to identify a potent nonapeptide inhibitor of human pancreatic α-amylase with high selectivity over other glycosidases.
    • 56• Jongkees, S.A.K., Caner, S., Tysoe, C., Brayer, G.D., Withers, S.G., Suga, H., Rapid discovery of potent and selective glycosidase-inhibiting de novo peptides. Cell Chem Biol, 2017, 10.1016/j.chembiol.2017.02.001 The authors use the RaPID system to identify a potent nonapeptide inhibitor of human pancreatic α-amylase with high selectivity over other glycosidases.
    • (2017) Cell Chem Biol
    • Jongkees, S.A.K.1    Caner, S.2    Tysoe, C.3    Brayer, G.D.4    Withers, S.G.5    Suga, H.6
  • 59
    • 84960425701 scopus 로고    scopus 로고
    • High-throughput measurement of binding kinetics by mRNA display and next-generation sequencing
    • D of selected peptides in addition to the rank order by enrichment level. Their method allowed them to identify higher affinity, but less enriched peptides that would not have been identified by traditional screening methods.
    • D of selected peptides in addition to the rank order by enrichment level. Their method allowed them to identify higher affinity, but less enriched peptides that would not have been identified by traditional screening methods.
    • (2016) Angew Chem Int Ed , vol.55 , pp. 4007-4010
    • Jalali-Yazdi, F.1    Lai, L.H.2    Takahashi, T.T.3    Roberts, R.W.4
  • 60
    • 84985914489 scopus 로고    scopus 로고
    • Peptide synthesis on a next-generation DNA sequencing platform
    • On an Illumina sequencing chip, DNA clusters were transcribed into RNA and translated into peptides, both being immobilised to the original DNA cluster. This platform sets the stage for massive parallel peptide screening.
    • 60•• Svensen, N., Peersen, O.B., Jaffrey, S.R., Peptide synthesis on a next-generation DNA sequencing platform. ChemBioChem 17 (2016), 1628–1635 On an Illumina sequencing chip, DNA clusters were transcribed into RNA and translated into peptides, both being immobilised to the original DNA cluster. This platform sets the stage for massive parallel peptide screening.
    • (2016) ChemBioChem , vol.17 , pp. 1628-1635
    • Svensen, N.1    Peersen, O.B.2    Jaffrey, S.R.3
  • 61
    • 84994009729 scopus 로고    scopus 로고
    • Passive membrane permeability in cyclic peptomer scaffolds is robust to extensive variation in side chain functionality and backbone geometry
    • 61 Furukawa, A., Townsend, C.E., Schwochert, J., Pye, C.R., Bednarek, M.A., Lokey, R.S., Passive membrane permeability in cyclic peptomer scaffolds is robust to extensive variation in side chain functionality and backbone geometry. J Med Chem 59 (2016), 9503–9512.
    • (2016) J Med Chem , vol.59 , pp. 9503-9512
    • Furukawa, A.1    Townsend, C.E.2    Schwochert, J.3    Pye, C.R.4    Bednarek, M.A.5    Lokey, R.S.6
  • 62
    • 0026546880 scopus 로고
    • Screening for receptor ligands using large libraries of peptides linked to the C terminus of the lac repressor
    • 62 Cull, M.G., Miller, J.F., Schatz, P.J., Screening for receptor ligands using large libraries of peptides linked to the C terminus of the lac repressor. Proc Natl Acad Sci U S A 89 (1992), 1865–1869.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 1865-1869
    • Cull, M.G.1    Miller, J.F.2    Schatz, P.J.3
  • 64
    • 0030994634 scopus 로고    scopus 로고
    • Yeast surface display for screening combinatorial polypeptide libraries
    • 64 Boder, E.T., Wittrup, K.D., Yeast surface display for screening combinatorial polypeptide libraries. Nat Biotechnol 15 (1997), 553–557.
    • (1997) Nat Biotechnol , vol.15 , pp. 553-557
    • Boder, E.T.1    Wittrup, K.D.2
  • 65
    • 0021818675 scopus 로고
    • Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface
    • 65 Smith, G.P., Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science 228 (1985), 1315–1317.
    • (1985) Science , vol.228 , pp. 1315-1317
    • Smith, G.P.1
  • 67
    • 0028592703 scopus 로고
    • An in vitro polysome display system for identifying ligands from very large peptide libraries
    • 67 Mattheakis, L.C., Bhattt, R.R., Dower, W.J., An in vitro polysome display system for identifying ligands from very large peptide libraries. Proc Natl Acad Sci U S A 91 (1994), 9022–9026.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 9022-9026
    • Mattheakis, L.C.1    Bhattt, R.R.2    Dower, W.J.3
  • 68
    • 84555190565 scopus 로고    scopus 로고
    • Natural product-like macrocyclic N-methyl-peptide inhibitors against a ubiquitin ligase uncovered from a ribosome-expressed de novo library
    • 68 Yamagishi, Y., Shoji, I., Miyagawa, S., Kawakami, T., Katoh, T., Goto, Y., Suga, H., Natural product-like macrocyclic N-methyl-peptide inhibitors against a ubiquitin ligase uncovered from a ribosome-expressed de novo library. Chem Biol 18 (2011), 1562–1570.
    • (2011) Chem Biol , vol.18 , pp. 1562-1570
    • Yamagishi, Y.1    Shoji, I.2    Miyagawa, S.3    Kawakami, T.4    Katoh, T.5    Goto, Y.6    Suga, H.7
  • 69
    • 84876021006 scopus 로고    scopus 로고
    • TRAP display: a high-speed selection method for the generation of functional polypeptides
    • 69 Ishizawa, T., Kawakami, T., Reid, P.C., Murakami, H., TRAP display: a high-speed selection method for the generation of functional polypeptides. J Am Chem Soc 135 (2013), 5433–5440.
    • (2013) J Am Chem Soc , vol.135 , pp. 5433-5440
    • Ishizawa, T.1    Kawakami, T.2    Reid, P.C.3    Murakami, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.