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Volumn 421, Issue 1, 2012, Pages 299-307

Internally quenched fluorescent peptide libraries with randomized sequences designed to detect endopeptidases

Author keywords

Cathepsin; Chymotrypsin; Combinatorial libraries; Dengue; Energy transfer peptides; Eqolisin; Pepsin; Peptide libraries; Protease; Substrate specificity; Trypsin

Indexed keywords

AMINO ACIDS; BACTERIOLOGY; BIOSYNTHESIS; CHLOROACETIC ACID; ENERGY TRANSFER; FORSTER RESONANCE ENERGY TRANSFER; PEPTIDES; SUBSTRATES; VIRUSES;

EID: 84855903151     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2011.10.025     Document Type: Article
Times cited : (24)

References (46)
  • 1
    • 17244364283 scopus 로고    scopus 로고
    • Proteases universally recognize beta strands in their active sites
    • DOI 10.1021/cr040669e
    • J.D.A. Tyndall, T. Nall, and D.P. Fairlie Proteases universally recognize beta strands in their active sites Chem. Rev. 105 2005 973 999 (Pubitemid 40527381)
    • (2005) Chemical Reviews , vol.105 , Issue.3 , pp. 973-999
    • Tyndall, J.D.A.1    Nall, T.2    Fairlie, D.P.3
  • 2
    • 33748308883 scopus 로고    scopus 로고
    • Targeting proteases: Successes, failures and future prospects
    • DOI 10.1038/nrd2092, PII NRD2092
    • B. Turk Targeting proteases: successes, failures and future prospects Nat. Rev. Drug Discov. 5 2006 785 799 (Pubitemid 44323703)
    • (2006) Nature Reviews Drug Discovery , vol.5 , Issue.9 , pp. 785-799
    • Turk, B.1
  • 3
    • 0036890336 scopus 로고    scopus 로고
    • Scanning the prime-Site substrate specificity of proteolytic enzymes: A novel assay based on ligand-Enhanced lanthanide ion fluorescence
    • DOI 10.1016/S0960-894X(02)00786-2, PII S0960894X02007862
    • A.M. Barrios, and C.S. Craik Scanning the prime-site substrate specificity of proteolytic enzymes: a novel assay based on ligand-enhanced lanthanide ion fluorescence Bioorg. Med. Chem. Lett. 12 2002 3619 3623 (Pubitemid 35346501)
    • (2002) Bioorganic and Medicinal Chemistry Letters , vol.12 , Issue.24 , pp. 3619-3623
    • Barrios, A.M.1    Craik, C.S.2
  • 5
    • 57649155302 scopus 로고    scopus 로고
    • Proteases: Multifunctional enzymes in life and disease
    • C. Lopez-Otin, and J.S. Bond Proteases: multifunctional enzymes in life and disease J. Biol. Chem. 283 2008 30433 30437
    • (2008) J. Biol. Chem. , vol.283 , pp. 30433-30437
    • Lopez-Otin, C.1    Bond, J.S.2
  • 7
    • 70349303457 scopus 로고    scopus 로고
    • The use of fluorescence resonance energy transfer (FRET) peptides for measurement of clinically important proteolytic enzymes
    • A.K. Carmona, M.A. Juliano, and L. Juliano The use of fluorescence resonance energy transfer (FRET) peptides for measurement of clinically important proteolytic enzymes An. Acad. Bras. Cienc. 81 2009 381 392
    • (2009) An. Acad. Bras. Cienc. , vol.81 , pp. 381-392
    • Carmona, A.K.1    Juliano, M.A.2    Juliano, L.3
  • 8
    • 0033951198 scopus 로고    scopus 로고
    • Synthesis of positional-scanning libraries of fluorogenic peptide substrates to define the extended substrate specificity of plasmin and thrombin
    • DOI 10.1038/72642
    • B.J. Backes, J.L. Harris, F. Leonetti, C.S. Craik, and J.A. Ellman Synthesis of positional-scanning libraries of fluorogenic peptide substrates to define the extended substrate specificity of plasmin and thrombin Nat. Biotechnol. 18 2000 187 193 (Pubitemid 30091180)
    • (2000) Nature Biotechnology , vol.18 , Issue.2 , pp. 187-193
    • Backes, B.J.1    Harris, J.L.2    Leonetti, F.3    Craik, C.S.4    Ellman, J.A.5
  • 10
    • 0034946412 scopus 로고    scopus 로고
    • Determination of protease cleavage site motifs using mixture-based oriented peptide libraries
    • DOI 10.1038/90273
    • B.E. Turk, L.L. Huang, E.T. Piro, and L.C. Cantley Determination of protease cleavage site motifs using mixture-based oriented peptide libraries Nat. Biotechnol. 19 2001 661 667 (Pubitemid 32625438)
    • (2001) Nature Biotechnology , vol.19 , Issue.7 , pp. 661-667
    • Turk, B.E.1    Huang, L.L.2    Piro, E.T.3    Cantley, L.C.4
  • 11
    • 1542315414 scopus 로고    scopus 로고
    • Using peptide libraries to identify optimal cleavage motifs for proteolytic enzymes
    • DOI 10.1016/j.ymeth.2003.10.003, PII S104620230300269X
    • B.E. Turk, and L.C. Cantley Using peptide libraries to identify optimal cleavage motifs for proteolytic enzymes Methods 32 2004 398 405 (Pubitemid 38299331)
    • (2004) Methods , vol.32 , Issue.4 , pp. 398-405
    • Turk, B.E.1    Cantley, L.C.2
  • 13
    • 34547218898 scopus 로고    scopus 로고
    • Controlled peptide solvation in portion-mixing libraries of FRET peptides: Improved specificity determination for dengue 2 virus NS2B-NS3 protease and human cathepsin S
    • M.A. Juliano, F.M. Alves, I.Y. Hirata, I.E. Gouvea, M.F.M. Alves, M. Meldal, D. Bromme, and L. Juliano Controlled peptide solvation in portion-mixing libraries of FRET peptides: improved specificity determination for dengue 2 virus NS2B-NS3 protease and human cathepsin S J. Comb. Chem. 9 2007 627 634
    • (2007) J. Comb. Chem. , vol.9 , pp. 627-634
    • Juliano, M.A.1    Alves, F.M.2    Hirata, I.Y.3    Gouvea, I.E.4    Alves, M.F.M.5    Meldal, M.6    Bromme, D.7    Juliano, L.8
  • 15
    • 0028567973 scopus 로고
    • Characterization of the peptide substrate specificities of interstitial collagenase and 92-kDa gelatinase. Implications for substrate optimization
    • G.M. McGeehan, D.M. Bickett, M. Green, D. Kassel, J.S. Wiseman, and J.J. Berman Characterization of the peptide substrate specificities of interstitial collagenase and 92-kDa gelatinase. Implications for substrate optimization J. Biol. Chem. 269 1994 32814 32820
    • (1994) J. Biol. Chem. , vol.269 , pp. 32814-32820
    • McGeehan, G.M.1    Bickett, D.M.2    Green, M.3    Kassel, D.4    Wiseman, J.S.5    Berman, J.J.6
  • 16
    • 0027190868 scopus 로고
    • Mapping the S' subsites of serine proteases using acyl transfer to mixtures of peptide nucleophiles
    • V. Schellenberger, C.W. Turck, L. Hedstrom, and W.J. Rutter Mapping the S′-subsites of serine proteases using acyl transfer to mixtures of peptide nucleophiles Biochemistry 32 1993 4349 4353 (Pubitemid 23137744)
    • (1993) Biochemistry , vol.32 , Issue.16 , pp. 4349-4353
    • Schellenberger, V.1    Turck, C.W.2    Hedstrom, L.3    Rutter, W.J.4
  • 19
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • I. Schechter, and A. Berger On the size of the active site in proteases. I. Papain Biochem. Biophys. Res. Commun. 27 1967 157 162
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 24
    • 84855863298 scopus 로고    scopus 로고
    • Amylolytic microorganism from São Paulo zoo composting: Isolation, identification, and amylase production
    • 10.4061/2011/679624
    • R.C. Pascon, R.F. Bergamo, R.X. Spinelli, E.D. de Souza, D.M. Assis, L. Juliano, and M.A. Vallim Amylolytic microorganism from São Paulo zoo composting: isolation, identification, and amylase production Enzyme Res. 2011 10.4061/2011/679624
    • (2011) Enzyme Res.
    • Pascon, R.C.1    Bergamo, R.F.2    Spinelli, R.X.3    De Souza, E.D.4    Assis, D.M.5    Juliano, L.6    Vallim, M.A.7
  • 26
    • 0040366645 scopus 로고    scopus 로고
    • Human cathepsin X: A cysteine protease with unique carboxypeptidase activity
    • D.K. Nagler, R. Zhang, W. Tam, T. Sulea, E.O. Purisima, and R. Menard Human cathepsin X: a cysteine protease with unique carboxypeptidase activity Biochemistry 38 1999 12648 12654
    • (1999) Biochemistry , vol.38 , pp. 12648-12654
    • Nagler, D.K.1    Zhang, R.2    Tam, W.3    Sulea, T.4    Purisima, E.O.5    Menard, R.6
  • 27
    • 44949182000 scopus 로고    scopus 로고
    • Measuring elastase, proteinase 3 and cathepsin G activities at the surface of human neutrophils with fluorescence resonance energy transfer substrates
    • DOI 10.1038/nprot.2008.63, PII NPROT.2008.63
    • B. Korkmaz, S. Attucci, M.A. Juliano, T. Kalupov, M.L. Jourdan, L. Juliano, and F. Gauthier Measuring elastase, proteinase 3 and cathepsin G activities at the surface of human neutrophils with fluorescence resonance energy transfer substrates Nat. Protoc. 3 2008 991 1000 (Pubitemid 351818687)
    • (2008) Nature Protocols , vol.3 , Issue.6 , pp. 991-1000
    • Korkmaz, B.1    Attucci, S.2    Juliano, M.A.3    Kalupov, T.4    Jourdan, M.-L.5    Juliano, L.6    Gauthier, F.7
  • 28
    • 0028172455 scopus 로고
    • Peptide libraries: Determination of relative reaction rates of protected amino acids in competitive couplings
    • DOI 10.1002/bip.360341212
    • J.M. Ostresh, J.H. Winkle, V.T. Hamashin, and R.A. Houghten Peptide libraries: determination of relative reaction rates of protected amino acids in competitive couplings Biopolymers 34 1994 1681 1689 (Pubitemid 24357583)
    • (1994) Biopolymers , vol.34 , Issue.12 , pp. 1681-1689
    • Ostresh, J.M.1    Winkle, J.H.2    Hamashin, V.T.3    Houghten, R.A.4
  • 29
    • 34547218898 scopus 로고    scopus 로고
    • Controlled peptide solvation in portion-mixing libraries of FRET peptides: Improved specificity determination for dengue 2 virus NS2B-NS3 protease and human cathepsin S
    • F.M. Alves, I.Y. Hirata, I.E. Gouvea, M.F.M. Alves, M. Meldal, D. Bromme, L. Juliano, and M.A. Juliano Controlled peptide solvation in portion-mixing libraries of FRET peptides: improved specificity determination for dengue 2 virus NS2B-NS3 protease and human cathepsin S J. Comb. Chem. 9 2007 627 634
    • (2007) J. Comb. Chem. , vol.9 , pp. 627-634
    • Alves, F.M.1    Hirata, I.Y.2    Gouvea, I.E.3    Alves, M.F.M.4    Meldal, M.5    Bromme, D.6    Juliano, L.7    Juliano, M.A.8
  • 31
    • 0021827776 scopus 로고
    • Redesigning trypsin: Alteration of substrate specificity
    • C.S. Craik, C. Largman, T. Fletcher, S. Roczniak, P.J. Barr, R. Fletterick, and W.J. Rutter Redesigning tryps: alteration of substrate specificity Science 228 1985 291 297 (Pubitemid 15076825)
    • (1985) Science , vol.228 , Issue.4697 , pp. 291-297
    • Craik, C.S.1    Largman, C.2    Fletcher, T.3
  • 32
    • 33846872163 scopus 로고    scopus 로고
    • Methods for mapping protease specificity
    • DOI 10.1016/j.cbpa.2006.11.021, PII S1367593106001852
    • S.L. Diamond Methods for mapping protease specificity Curr. Opin. Chem. Biol. 11 2007 46 51 (Pubitemid 46223545)
    • (2007) Current Opinion in Chemical Biology , vol.11 , Issue.1 , pp. 46-51
    • Diamond, S.L.1
  • 35
    • 0035660408 scopus 로고    scopus 로고
    • Comparison of the specificity, stability and individual rate constants with respective activation parameters for the peptidase activity of cruzipain and its recombinant form, cruzain, from trypanosoma cruzi
    • DOI 10.1046/j.0014-2956.2001.02612.x
    • W.A. Judice, M.H. Cezari, A.P. Lima, J. Scharfstein, J.R. Chagas, I.L. Tersariol, M.A. Juliano, and L. Juliano Comparison of the specificity, stability and individual rate constants with respective activation parameters for the peptidase activity of cruzipain and its recombinant form, cruzain, from Trypanosoma cruzi Eur. J. Biochem. 268 2001 6578 6586 (Pubitemid 34014765)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.24 , pp. 6578-6586
    • Judice, W.A.S.1    Cezari, M.H.S.2    Lima, A.P.C.A.3    Scharfstein, J.4    Chagas, J.R.5    Tersariol, I.L.S.6    Juliano, M.A.7    Juliano, L.8
  • 36
    • 0034745154 scopus 로고    scopus 로고
    • 1 subsite specificity of a recombinant cysteine proteinase, CPB, of Leishmania mexicana compared with cruzain, human cathepsin L and papain using substrates containing non-natural basic amino acids
    • DOI 10.1046/j.1432-1327.2001.01973.x
    • L.C. Alves, R.L. Melo, S.J. Sanderson, J.C. Mottram, G.H. Coombs, G. Caliendo, V. Santagada, L. Juliano, and M.A. Juliano S1 subsite specificity of a recombinant cysteine proteinase, CPB, of Leishmania mexicana compared with cruzain, human cathepsin L and papain using substrates containing non-natural basic amino acids Eur. J. Biochem. 268 2001 1206 1212 (Pubitemid 32231872)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.5 , pp. 1206-1212
    • Alves, L.C.1    Melo, R.L.2    Sanderson, S.J.3    Mottram, J.C.4    Coombs, G.H.5    Caliendo, G.6    Santagada, V.7    Juliano, L.8    Juliano, M.A.9
  • 37
    • 34547745385 scopus 로고    scopus 로고
    • Processing of capsid protein by cathepsin L plays a crucial role in replication of Japanese encephalitis virus in neural and macrophage cells
    • DOI 10.1128/JVI.00477-07
    • Y. Mori, T. Yamashita, Y. Tanaka, Y. Tsuda, T. Abe, K. Moriishi, and Y. Matsuura Processing of capsid protein by cathepsin L plays a crucial role in replication of Japanese encephalitis virus in neural and macrophage cells J. Virol. 81 2007 8477 8487 (Pubitemid 47242820)
    • (2007) Journal of Virology , vol.81 , Issue.16 , pp. 8477-8487
    • Mori, Y.1    Yamashita, T.2    Tanaka, Y.3    Tsuda, Y.4    Abe, T.5    Moriishi, K.6    Matsuura, Y.7
  • 41
    • 20444398543 scopus 로고    scopus 로고
    • Catalytic residues and substrate specificity of scytalidoglutamic peptidase, the first member of the eqolisin in family (G1) of peptidases
    • DOI 10.1016/j.febslet.2005.04.050, PII S0014579305005259
    • Y. Kataoka, K. Takada, H. Oyama, M. Tsunemi, M.N.G. James, and K. Oda Catalytic residues and substrate specificity of scytalidoglutamic peptidase, the first member of the eqolisin in family (G1) of peptidases FEBS Lett. 579 2005 2991 2994 (Pubitemid 40797824)
    • (2005) FEBS Letters , vol.579 , Issue.14 , pp. 2991-2994
    • Kataoka, Y.1    Takada, K.2    Oyama, H.3    Tsunemi, M.4    James, M.N.G.5    Oda, K.6
  • 42
    • 67649617069 scopus 로고    scopus 로고
    • Subsite cooperativity in protease specificity
    • N.M. Ng, R.N. Pike, and S.E. Boyd Subsite cooperativity in protease specificity Biol. Chem. 390 2009 401 407
    • (2009) Biol. Chem. , vol.390 , pp. 401-407
    • Ng, N.M.1    Pike, R.N.2    Boyd, S.E.3
  • 43
    • 0036882390 scopus 로고    scopus 로고
    • Structure and mechanism of the pepsin-like family of aspartic peptidases
    • B.M. Dunn Structure and mechanism of the pepsin-like family of aspartic peptidases Chem. Rev. 102 2002 4431 4458
    • (2002) Chem. Rev. , vol.102 , pp. 4431-4458
    • Dunn, B.M.1
  • 44
    • 0035824539 scopus 로고    scopus 로고
    • Activity of recombinant dengue 2 virus NS3 protease in the presence of a truncated NS2B co-factor, small peptide substrates, and inhibitors
    • D. Leung, K. Schroder, H. White, N.X. Fang, M.J. Stoermer, G. Abbenante, J.L. Martin, P.R. Young, and D.P. Fairlie Activity of recombinant dengue 2 virus NS3 protease in the presence of a truncated NS2B co-factor, small peptide substrates, and inhibitors J. Biol. Chem. 276 2001 45762 45771
    • (2001) J. Biol. Chem. , vol.276 , pp. 45762-45771
    • Leung, D.1    Schroder, K.2    White, H.3    Fang, N.X.4    Stoermer, M.J.5    Abbenante, G.6    Martin, J.L.7    Young, P.R.8    Fairlie, D.P.9
  • 45
    • 31144449876 scopus 로고    scopus 로고
    • Substrate specificity of insect trypsins and the role of their subsites in catalysis
    • DOI 10.1016/j.ibmb.2005.11.006, PII S0965174805002122
    • A.R. Lopes, M.A. Juliano, S.R. Marana, L. Juliano, and W.R. Terra Substrate specificity of insect trypsins and the role of their subsites in catalysis Insect Biochem. Mol. Biol. 36 2006 130 140 (Pubitemid 43129405)
    • (2006) Insect Biochemistry and Molecular Biology , vol.36 , Issue.2 , pp. 130-140
    • Lopes, A.R.1    Juliano, M.A.2    Marana, S.R.3    Juliano, L.4    Terra, W.R.5
  • 46
    • 0016914760 scopus 로고
    • Mechanism of catalytic action of pepsin and related acid proteinases
    • J.S. Fruton Mechanism of catalytic action of pepsin and related acid proteinases Adv. Enzymol. Relat. Areas Mol. Biol. 44 1976 1 36
    • (1976) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.44 , pp. 1-36
    • Fruton, J.S.1


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