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Volumn 292, Issue 2, 1999, Pages 421-429

Miniaturized proteins: The backbone cyclic proteinomimetic approach

Author keywords

Backbone cyclic peptides; Backbone cyclization; Bovine pancreatic trypsin inhibitor; Cycloscan; Proteinomimetic

Indexed keywords

APROTININ; CYCLOPEPTIDE; NONAPEPTIDE; TRYPSIN;

EID: 0033578941     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3053     Document Type: Article
Times cited : (47)

References (61)
  • 1
    • 0025980302 scopus 로고
    • Synthesis of cystine-peptide by a new disulphide bond-forming reaction using the silyl chloride-sulphoxide system
    • Akaji K., Tatsumi T., Yoshida M., Kimura T., Fujiwara Y., Kiso Y. Synthesis of cystine-peptide by a new disulphide bond-forming reaction using the silyl chloride-sulphoxide system. J. Chem. Soc. Chem. Commun. 1991;167-168.
    • (1991) J. Chem. Soc. Chem. Commun. , pp. 167-168
    • Akaji, K.1    Tatsumi, T.2    Yoshida, M.3    Kimura, T.4    Fujiwara, Y.5    Kiso, Y.6
  • 2
    • 0026763134 scopus 로고
    • Disulfide bond formation using the silyl chloride-sulfoxide system for the synthesis of a cystine peptide
    • Akaji K., Tatsumi T., Yoshida M., Kimura T., Fujiwara Y., Kiso Y. Disulfide bond formation using the silyl chloride-sulfoxide system for the synthesis of a cystine peptide. J. Am. Chem. Soc. 114:1992;4137-4143.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 4137-4143
    • Akaji, K.1    Tatsumi, T.2    Yoshida, M.3    Kimura, T.4    Fujiwara, Y.5    Kiso, Y.6
  • 5
    • 0026530977 scopus 로고
    • Natural protein proteinase inhibitors and their interaction with proteinases
    • Bode W., Huber R. Natural protein proteinase inhibitors and their interaction with proteinases. Annu. Rev. Biochem. 204:1992;433-451.
    • (1992) Annu. Rev. Biochem. , vol.204 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 6
    • 0029904435 scopus 로고    scopus 로고
    • Minimizing a binding domain from protein A
    • Braisted A. C., Wells J. A. Minimizing a binding domain from protein A. Proc. Natl Acad. Sci. USA. 93:1996;5688-5692.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 5688-5692
    • Braisted, A.C.1    Wells, J.A.2
  • 9
    • 0029742789 scopus 로고    scopus 로고
    • Synthesis and biological activity of NK-1 selective, N-backbone cyclic analogs of the C-terminal hexapeptide of Substance P
    • Byk G., Halle D., Zeltser I., Bitan G., Selinger Z., Gilon C. Synthesis and biological activity of NK-1 selective, N-backbone cyclic analogs of the C-terminal hexapeptide of Substance P. J. Med. Chem. 39:1996;3174-3178.
    • (1996) J. Med. Chem. , vol.39 , pp. 3174-3178
    • Byk, G.1    Halle, D.2    Zeltser, I.3    Bitan, G.4    Selinger, Z.5    Gilon, C.6
  • 10
    • 0020645978 scopus 로고
    • Refined 2.5 Å X-ray crystal structure of the complex formed by porcine kallikrein A and the bovine pancreatic trypsin inhibitor
    • Chen Z., Bode W. Refined 2.5 Å X-ray crystal structure of the complex formed by porcine kallikrein A and the bovine pancreatic trypsin inhibitor. J. Mol. Biol. 164:1983;283-311.
    • (1983) J. Mol. Biol. , vol.164 , pp. 283-311
    • Chen, Z.1    Bode, W.2
  • 12
    • 0028670569 scopus 로고
    • In vivo repression by a site-specific DNA-binding protein designed against an oncogenic sequence
    • Choo Y., Sanchez-Garcia I., Klug A. In vivo repression by a site-specific DNA-binding protein designed against an oncogenic sequence. Nature. 372:1994;642-645.
    • (1994) Nature , vol.372 , pp. 642-645
    • Choo, Y.1    Sanchez-Garcia, I.2    Klug, A.3
  • 15
    • 0029969102 scopus 로고    scopus 로고
    • On the failure of de novo -designed peptides as biocatalysts
    • Corey M. J., Corey E. On the failure of de novo -designed peptides as biocatalysts. Proc. Natl Acad. Sci. USA. 93:1996;11428-11434.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 11428-11434
    • Corey, M.J.1    Corey, E.2
  • 17
    • 0030793767 scopus 로고    scopus 로고
    • De novo protein design: Fully automated sequence selection
    • Dahiyat B. I., Mayo S. L. De novo protein design: fully automated sequence selection. Science. 278:1997;82-87.
    • (1997) Science , vol.278 , pp. 82-87
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 18
    • 0031558762 scopus 로고    scopus 로고
    • De novo protein design: Towards fully automated sequence selection
    • Dahiyat B. I., Sarisky C. A., Mayo S. L. De novo protein design: towards fully automated sequence selection. J. Mol. Biol. 273:1997;789-796.
    • (1997) J. Mol. Biol. , vol.273 , pp. 789-796
    • Dahiyat, B.I.1    Sarisky, C.A.2    Mayo, S.L.3
  • 19
    • 0024515763 scopus 로고
    • Protein design, a minimalist approach
    • DeGrado W. F., Wasserman Z. R., Lear J. D. Protein design, a minimalist approach. Science. 243:1989;622-628.
    • (1989) Science , vol.243 , pp. 622-628
    • Degrado, W.F.1    Wasserman, Z.R.2    Lear, J.D.3
  • 20
    • 0001612915 scopus 로고
    • Crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor at 1.5 Å resolution
    • Deisenhofer J., Steigemann W. Crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor at 1.5 Å resolution. Acta Crystallog. sect. B. 31:1975;238-250.
    • (1975) Acta Crystallog. Sect. B , vol.31 , pp. 238-250
    • Deisenhofer, J.1    Steigemann, W.2
  • 21
    • 0029034507 scopus 로고
    • Synthesis of a mixture of cyclic peptides based on the Bowman-Birk reactive site loop to screen for serine protease inhibitors
    • Domingo G. J., Leatherbarrow R. J., Freeman N., Patel S., Weir M. Synthesis of a mixture of cyclic peptides based on the Bowman-Birk reactive site loop to screen for serine protease inhibitors. Int. J. Peptide Protein Res. 46:1995;79-87.
    • (1995) Int. J. Peptide Protein Res. , vol.46 , pp. 79-87
    • Domingo, G.J.1    Leatherbarrow, R.J.2    Freeman, N.3    Patel, S.4    Weir, M.5
  • 22
    • 0027454521 scopus 로고
    • Identification of substrate-analog trypsin inhibitors through the screening of synthetic peptide combinatorial libraries
    • Eichler J., Houghten R. A. Identification of substrate-analog trypsin inhibitors through the screening of synthetic peptide combinatorial libraries. Biochemistry. 32:1993;11035-11041.
    • (1993) Biochemistry , vol.32 , pp. 11035-11041
    • Eichler, J.1    Houghten, R.A.2
  • 24
    • 0032554629 scopus 로고    scopus 로고
    • Backbone cyclic peptide which mimics the nuclear import of HIV-1 matrix protein inhibits nuclear import and virus reproduction in non-dividing cells
    • Friedler A., Zakai N., Karni O., Broder Y. C., Baraz L., Loyter A., Kotler M., Gilon C. Backbone cyclic peptide which mimics the nuclear import of HIV-1 matrix protein inhibits nuclear import and virus reproduction in non-dividing cells. Biochemistry. 37:1998;5616-5622.
    • (1998) Biochemistry , vol.37 , pp. 5616-5622
    • Friedler, A.1    Zakai, N.2    Karni, O.3    Broder, Y.C.4    Baraz, L.5    Loyter, A.6    Kotler, M.7    Gilon, C.8
  • 26
    • 0002934213 scopus 로고
    • Biochemistry of aprotinin and aprotinin-like inhibitors
    • A. J. Barrett, & G. Salvesen. Amsterdam: Elsevier Science
    • Gebhard W., Tschesche H., Fritz H. Biochemistry of aprotinin and aprotinin-like inhibitors. Barrett A. J., Salvesen G. Proteinase Inhibitors. 1986;375-389 Elsevier Science, Amsterdam.
    • (1986) Proteinase Inhibitors , pp. 375-389
    • Gebhard, W.1    Tschesche, H.2    Fritz, H.3
  • 28
    • 0026155124 scopus 로고
    • Backbone cyclization: A new method for conferring conformational constraint on peptides
    • Gilon C., Halle D., Chorev M., Selinger Z., Byk G. Backbone cyclization: a new method for conferring conformational constraint on peptides. Biopolymers. 31:1991;745-750.
    • (1991) Biopolymers , vol.31 , pp. 745-750
    • Gilon, C.1    Halle, D.2    Chorev, M.3    Selinger, Z.4    Byk, G.5
  • 30
    • 0025040232 scopus 로고
    • De novo design, expression and characterization of Felix: A four-helix bundle protein of native-like sequence
    • Hecht M. H., Richardson J. S., Richardson D. C., Ogden R. C. De novo design, expression and characterization of Felix: A four-helix bundle protein of native-like sequence. Science. 249:1990;884-891.
    • (1990) Science , vol.249 , pp. 884-891
    • Hecht, M.H.1    Richardson, J.S.2    Richardson, D.C.3    Ogden, R.C.4
  • 31
    • 0000478940 scopus 로고
    • General method for the rapid solid-phase synthesis of large numbers of peptides: Specificity of antigen-antibody interaction at the level of individual amino acids
    • Houghten R. General method for the rapid solid-phase synthesis of large numbers of peptides: Specificity of antigen-antibody interaction at the level of individual amino acids. Proc. Natl Acad. Sci. USA. 82:1985;5131-5135.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 5131-5135
    • Houghten, R.1
  • 32
    • 0027516857 scopus 로고
    • Refined 1.6 Å resolution crystal structure of the complex formed between porcine β-trypsin and MCTI-A, a trypsin inhibitor of the squash family
    • Huang Q., Liu S., Tang Y. Refined 1.6 Å resolution crystal structure of the complex formed between porcine β-trypsin and MCTI-A, a trypsin inhibitor of the squash family. J. Mol. Biol. 229:1993;1022-1036.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1022-1036
    • Huang, Q.1    Liu, S.2    Tang, Y.3
  • 33
    • 33947092515 scopus 로고
    • Structural basis of the activation and action of trypsin
    • Huber R., Bode W. Structural basis of the activation and action of trypsin. Accts. Chem. Res. 11:1978;114-122.
    • (1978) Accts. Chem. Res. , vol.11 , pp. 114-122
    • Huber, R.1    Bode, W.2
  • 34
    • 0026206788 scopus 로고
    • Sparce matrix sampling: A screening method for crystallization of proteins
    • Jancarik J., Kim S. H. Sparce matrix sampling: a screening method for crystallization of proteins. J. Appl. Crystallog. 24:1991;409-411.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 409-411
    • Jancarik, J.1    Kim, S.H.2
  • 35
    • 0017257628 scopus 로고
    • Stability and specificity of protein-protein interactions: The case of the trypsin-trypsin inhibitor complexes
    • Janin J., Chothia C. Stability and specificity of protein-protein interactions: The case of the trypsin-trypsin inhibitor complexes. J. Mol. Biol. 100:1976;197-211.
    • (1976) J. Mol. Biol. , vol.100 , pp. 197-211
    • Janin, J.1    Chothia, C.2
  • 36
    • 0031554927 scopus 로고    scopus 로고
    • Quenched BODIPY dye-labeled casein substrates for the assay of protease activity by direct fluorescence measurement
    • Jones L. J., Upson R. H., Haugland R. P., Panchuk-Voloshina N., Zhou M., Haugland R. P. Quenched BODIPY dye-labeled casein substrates for the assay of protease activity by direct fluorescence measurement. Anal. Biochem. 251:1997;144-152.
    • (1997) Anal. Biochem. , vol.251 , pp. 144-152
    • Jones, L.J.1    Upson, R.H.2    Haugland, R.P.3    Panchuk-Voloshina, N.4    Zhou, M.5    Haugland, R.P.6
  • 37
    • 0022333120 scopus 로고
    • Interactive computer graphics: FRODO
    • Jones T. A. Interactive computer graphics: FRODO. Methods Enzymol. 115:1985;157-171.
    • (1985) Methods Enzymol. , vol.115 , pp. 157-171
    • Jones, T.A.1
  • 38
    • 84943706546 scopus 로고
    • The synthesis of cystine peptides by iodine oxidation of S-trityl-cysteine and S-acetamidomethyl-cysteine peptides
    • Kamber B., Hartmann A., Eisler K., Riniker B., Rink H., Sieber P., Rittel W. The synthesis of cystine peptides by iodine oxidation of S-trityl-cysteine and S-acetamidomethyl-cysteine peptides. Helv. Chim. Acta. 63:1980;899-915.
    • (1980) Helv. Chim. Acta , vol.63 , pp. 899-915
    • Kamber, B.1    Hartmann, A.2    Eisler, K.3    Riniker, B.4    Rink, H.5    Sieber, P.6    Rittel, W.7
  • 40
    • 0002978054 scopus 로고
    • The characterization of enzyme inhibition
    • A. J. Barrett, & G. Salvesen. Amsterdam: Elsevier
    • Knight C. G. The characterization of enzyme inhibition. Barrett A. J., Salvesen G. Proteinase Inhibitors. 1986;23-51 Elsevier, Amsterdam.
    • (1986) Proteinase Inhibitors , pp. 23-51
    • Knight, C.G.1
  • 41
    • 2642670311 scopus 로고    scopus 로고
    • Design of a 20-amino acid, three stranded β-sheet protein
    • Kortemme T., Ramirez-Alvarado M., Serrano L. Design of a 20-amino acid, three stranded β-sheet protein. Science. 281:1998;253-256.
    • (1998) Science , vol.281 , pp. 253-256
    • Kortemme, T.1    Ramirez-Alvarado, M.2    Serrano, L.3
  • 43
    • 0026314941 scopus 로고
    • Design of a small peptide-based proteinase inhibitor by modeling the active-site region of barley chymotrypsin inhibitor 2
    • Leatherbarrow R. J., Salacinski H. J. Design of a small peptide-based proteinase inhibitor by modeling the active-site region of barley chymotrypsin inhibitor 2. Biochemistry. 30:1991;10717-10721.
    • (1991) Biochemistry , vol.30 , pp. 10717-10721
    • Leatherbarrow, R.J.1    Salacinski, H.J.2
  • 44
    • 0026699754 scopus 로고
    • Design and inhibitory properties of synthetic Bowman-Birk loops
    • Maeder D., Sunde M., Botes D. P. Design and inhibitory properties of synthetic Bowman-Birk loops. Int. J. Peptide Protein Res. 40:1992;97-102.
    • (1992) Int. J. Peptide Protein Res. , vol.40 , pp. 97-102
    • Maeder, D.1    Sunde, M.2    Botes, D.P.3
  • 45
    • 84977303841 scopus 로고
    • The geometry of the reactive site and of the peptide groups in trypsin, trypsinogen and its complexes with inhibitors
    • Marquart M., Walter J., Deisenhofer J., Bode W., Huber R. The geometry of the reactive site and of the peptide groups in trypsin, trypsinogen and its complexes with inhibitors. Acta Crystallog. sect. B. 39:1983;480-490.
    • (1983) Acta Crystallog. Sect. B , vol.39 , pp. 480-490
    • Marquart, M.1    Walter, J.2    Deisenhofer, J.3    Bode, W.4    Huber, R.5
  • 46
    • 0028349315 scopus 로고
    • Can small peptides have the activity and specificity of proteolytic enzymes?
    • Matthews B. W., Craik C. S., Neurath H. Can small peptides have the activity and specificity of proteolytic enzymes? Proc. Natl Acad. Sci. USA. 91:1994;4103-4105.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 4103-4105
    • Matthews, B.W.1    Craik, C.S.2    Neurath, H.3
  • 48
    • 0024665396 scopus 로고
    • A chemical approach to protein design- Template-Assembled Synthetic Proteins (TASP)
    • Mutter M., Vuilleumier S. A chemical approach to protein design- Template-Assembled Synthetic Proteins (TASP). Angew. Chem. Int. Ed. Eng. 28:1989;535-676.
    • (1989) Angew. Chem. Int. Ed. Eng. , vol.28 , pp. 535-676
    • Mutter, M.1    Vuilleumier, S.2
  • 49
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1996;307-325.
    • (1996) Methods Enzymol. , vol.276 , pp. 307-325
    • Otwinowski, Z.1    Minor, W.2
  • 50
    • 0014011074 scopus 로고
    • The reactive site of trypsin inhibitors
    • Ozawa K., Laskowski M. Jr. The reactive site of trypsin inhibitors. J. Biol. Chem. 241:1966;3955-3961.
    • (1966) J. Biol. Chem. , vol.241 , pp. 3955-3961
    • Ozawa, K.1    Laskowski M., Jr.2
  • 52
    • 0029016430 scopus 로고
    • Protein design: Novel metal-binding sites
    • Regan L. Protein design: novel metal-binding sites. Trends Biochem. Sci. 20:1995;280-285.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 280-285
    • Regan, L.1
  • 53
    • 0015901579 scopus 로고
    • Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Crystal structure determination and stereochemistry of the contact residues
    • Ruhlmann A., Kukla D., Schwager P., Bartels K., Huber R. Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Crystal structure determination and stereochemistry of the contact residues. J. Mol. Biol. 77:1973;417-436.
    • (1973) J. Mol. Biol. , vol.77 , pp. 417-436
    • Ruhlmann, A.1    Kukla, D.2    Schwager, P.3    Bartels, K.4    Huber, R.5
  • 55
    • 0003518480 scopus 로고
    • New York: John Wiley & Sons. p. 161-226
    • Segel I. H. Enzyme Kinetics. 1975;John Wiley & Sons, New York. p. 161-226.
    • (1975) Enzyme Kinetics
    • Segel, I.H.1
  • 56
    • 0030593029 scopus 로고    scopus 로고
    • Design of a monomeric 23-residue polypeptide with defined tertiary structure
    • Struthers M. D., Cheng R. P., Imperiali B. Design of a monomeric 23-residue polypeptide with defined tertiary structure. Science. 271:1996;342-345.
    • (1996) Science , vol.271 , pp. 342-345
    • Struthers, M.D.1    Cheng, R.P.2    Imperiali, B.3
  • 57
    • 0017364950 scopus 로고
    • Synthesis and characterization of a pancreatic trypsin inhibitor homologue and a model inhibitor
    • Tan N. H., Kaiser E. T. Synthesis and characterization of a pancreatic trypsin inhibitor homologue and a model inhibitor. Biochemistry. 16:1977;1531-1541.
    • (1977) Biochemistry , vol.16 , pp. 1531-1541
    • Tan, N.H.1    Kaiser, E.T.2
  • 58
    • 0015387337 scopus 로고
    • Trypsin-pancreatic trypsin inhibitor association. Dynamics of the interaction and role of disulfide bridges
    • Vincent J. P., Lazdunski M. Trypsin-pancreatic trypsin inhibitor association. Dynamics of the interaction and role of disulfide bridges. Biochemistry. 11:1972;2967-2977.
    • (1972) Biochemistry , vol.11 , pp. 2967-2977
    • Vincent, J.P.1    Lazdunski, M.2


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