메뉴 건너뛰기




Volumn 17, Issue 10, 2010, Pages 1223-1227

Analogues of trypsin inhibitor SFTI-1 with disulfide bridge substituted by various length of carbonyl bridges

Author keywords

Carbonyl bridge; Inhibitors; Serine proteinases; Synthesis

Indexed keywords

CYCLOPEPTIDE; DISULFIDE; SFTI 1 PEPTIDE, SUNFLOWER; SFTI-1 PEPTIDE, SUNFLOWER; TRYPSIN; TRYPSIN INHIBITOR;

EID: 77958543512     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986610792231483     Document Type: Article
Times cited : (5)

References (26)
  • 3
    • 67649173112 scopus 로고    scopus 로고
    • Immobilized analogues of sunflower trypsin inhibitor-1 constitute a versatile group of affinity sorbents for selective isolation of serine proteases
    • Pereira, H.J.V.; salgado, M.C.O.; Oliveira, E.B. Immobilized analogues of sunflower trypsin inhibitor-1 constitute a versatile group of affinity sorbents for selective isolation of serine proteases. J. Chromatogr. B, 2009, 877, 2039-2044.
    • (2009) J. Chromatogr. B , vol.877 , pp. 2039-2044
    • Pereira, H.J.V.1    Salgado, M.C.O.2    Oliveira, E.B.3
  • 4
    • 79951557584 scopus 로고    scopus 로고
    • In vivo bio-synthesis of an Ala-scan library based on the cyclic peptide SFTI-1
    • [Epub ahead of print]
    • Austin, J.; Kimura, R.H.; Woo, Y-H.; Camarero, J.A. In vivo bio-synthesis of an Ala-scan library based on the cyclic peptide SFTI-1. Amino Acids, 2009, [Epub ahead of print].
    • (2009) Amino Acids
    • Austin, J.1    Kimura, R.H.2    Woo, Y.-H.3    Camarero, J.A.4
  • 5
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter, I.; Berger, A. On the size of the active site in proteases. I. Papain. Biochem. Bophys. Res. Commun., 1967, 27, 157-162.
    • (1967) Biochem. Bophys. Res. Commun , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 6
    • 0036290075 scopus 로고    scopus 로고
    • Chemical Synthesis and Kinetic Study of the Smallest Naturally Occurring Trypsin Inhibitor SFTI-1 Isolated from Sunflower Seeds and Its Analogues
    • Zabłotna, E.; Kaźmierczak, K.; Jaśkiewicz, A.; Stawikowski, M.; Kupryszewski, G.; Rolka, K. Chemical Synthesis and Kinetic Study of the Smallest Naturally Occurring Trypsin Inhibitor SFTI-1 Isolated from Sunflower Seeds and Its Analogues. Biochem. Biophys. Res. Commun., 2002, 292, 855-859.
    • (2002) Biochem. Biophys. Res. Commun , vol.292 , pp. 855-859
    • Zabłlotna, E.1    Kaźmierczak, K.2    Jaśkiewicz, A.3    Stawikowski, M.4    Kupryszewski, G.5    Rolka, K.6
  • 9
    • 65249101736 scopus 로고    scopus 로고
    • Introduction of non-natural amino acid residues into the substrate-specific P1 position of trypsin inhibitor SFTI-1 yields potent chymotrypsin and cathepsin G inhibitors
    • Łegowska, A.; Debowski, D.; Lesner, A.; Wysocka, M.; Rolka, K. Introduction of non-natural amino acid residues into the substrate-specific P1 position of trypsin inhibitor SFTI-1 yields potent chymotrypsin and cathepsin G inhibitors. Bioorg. Med. Chem., 2009, 17, 3302-3307.
    • (2009) Bioorg. Med. Chem , vol.17 , pp. 3302-3307
    • Legowska, A.1    Debowski, D.2    Lesner, A.3    Wysocka, M.4    Rolka, K.5
  • 10
    • 77149150054 scopus 로고    scopus 로고
    • Selection of peptomeric inhibitors of bovine-chymotrypsin and cathepsin G based on trypsin inhibitor SFTI-1 using combinatorial chemistry approach
    • Łegowska, A.; Debowski, D.; Lesner, A.; Wysocka, M.; Rolka, K. Selection of peptomeric inhibitors of bovine-chymotrypsin and cathepsin G based on trypsin inhibitor SFTI-1 using combinatorial chemistry approach. Mol. Divers., 2010, 14, 51-58.
    • (2010) Mol. Divers , vol.14 , pp. 51-58
    • Łegowska, A.1    Debowski, D.2    Lesner, A.3    Wysocka, M.4    Rolka, K.5
  • 11
    • 33845565683 scopus 로고    scopus 로고
    • Synthesis and Biological Activity of Seleno Sunflower Trypsin Inhibitor Analog
    • Guo, X.; Shi, J.; Tang, Z.; Cui, D. Synthesis and Biological Activity of Seleno Sunflower Trypsin Inhibitor Analog. Chem. Biol. Drug. Des., 2006, 68, 341-344.
    • (2006) Chem. Biol. Drug. Des , vol.68 , pp. 341-344
    • Guo, X.1    Shi, J.2    Tang, Z.3    Cui, D.4
  • 12
    • 33846436809 scopus 로고    scopus 로고
    • Design and Synthesis of Redox Stable Analogues of Sunflower Trypsin Inhibitors (SFTI-1) on Solid Support, Potent Inhibitors of Matriptase
    • Jiang, S.; Li, P.; Lee, S-L.; Lin, C.Y.; Long, Y-Q.; Johnson, M.D.; Dickson R.B.; Roller, P.P Design and Synthesis of Redox Stable Analogues of Sunflower Trypsin Inhibitors (SFTI-1) on Solid Support, Potent Inhibitors of Matriptase. Org. Lett., 2007, 9, 9-11.
    • (2007) Org. Lett , vol.9 , pp. 9-11
    • Jiang, S.1    Li, P.2    Lee, S.-L.3    Lin, C.Y.4    Long, Y.-Q.5    Johnson, M.D.6    Dickson, R.B.7    Roller, P.P.8
  • 13
    • 0031179212 scopus 로고    scopus 로고
    • Synthesis of a novel side-chain to side-chain cyclized enkephalin analogue containing a carbonyl bridge
    • Pawlak, D.; Chung, N.N.; Schiller, P.W.; Izdebski, J. Synthesis of a novel side-chain to side-chain cyclized enkephalin analogue containing a carbonyl bridge. J. Pept. Sci., 1997, 3, 277-281.
    • (1997) J. Pept. Sci , vol.3 , pp. 277-281
    • Pawlak, D.1    Chung, N.N.2    Schiller, P.W.3    Izdebski, J.4
  • 14
    • 0035060228 scopus 로고    scopus 로고
    • Highly potent side-chain to side- chain cyclized enkephalin analogues containing a carbonyl bridge: Synthesis, biology and conformation
    • Pawlak, D.; Oleszczuk, M.; Wójcik, J.; Pachulska, M.; Chung, N.N.; Schiller, P.W.; Izdebski, J. Highly potent side-chain to side- chain cyclized enkephalin analogues containing a carbonyl bridge: synthesis, biology and conformation. J. Pept. Sci., 2001, 7, 128-140.
    • (2001) J. Pept. Sci , vol.7 , pp. 128-140
    • Pawlak, D.1    Oleszczuk, M.2    Wójcik, J.3    Pachulska, M.4    Chung, N.N.5    Schiller, P.W.6    Izdebski, J.7
  • 19
    • 0027279553 scopus 로고
    • Automated allyl cleavage for continuous-flow synthesis of cyclic and branched peptides
    • Kates, S.A.; Daniels, S.B.; Albeticio, F. Automated allyl cleavage for continuous-flow synthesis of cyclic and branched peptides. Anal. Biochem., 1993, 212, 303-310.
    • (1993) Anal. Biochem , vol.212 , pp. 303-310
    • Kates, S.A.1    Daniels, S.B.2    Albeticio, F.3
  • 20
    • 0025014627 scopus 로고
    • PyBOP®: A new peptide coupling reagent devoid of toxic by-product
    • Coste, J.; Le-Nguyen, D.; Castro, B. PyBOP®: A new peptide coupling reagent devoid of toxic by-product. Tetrahedron Lett., 1990, 31, 205.
    • (1990) Tetrahedron Lett , vol.31 , pp. 205
    • Coste, J.1    Le-Nguyen, D.2    Castro, B.3
  • 21
    • 0032485517 scopus 로고    scopus 로고
    • Hydrazinolysis of Dde: Complete orthogonality with Aloc protecting groups
    • Rohwedder, B.; Mutti, Y.; Dumy, P.; Mutter, M. Hydrazinolysis of Dde: Complete orthogonality with Aloc protecting groups. Tetrahedron Lett., 1998, 39, 1175-1178.
    • (1998) Tetrahedron Lett , vol.39 , pp. 1175-1178
    • Rohwedder, B.1    Mutti, Y.2    Dumy, P.3    Mutter, M.4
  • 23
    • 33644864110 scopus 로고
    • P-Nitrophenyl-p'-guanidinobenzoate HCl: A new active site titrant for trypsin
    • Chase, T.; Schaw, E.M. Jr. p-Nitrophenyl-p'-guanidinobenzoate HCl: a new active site titrant for trypsin. Biochem. Biophys. Res. Commun., 1967, 29, 508-514.
    • (1967) Biochem. Biophys. Res. Commun , vol.29 , pp. 508-514
    • Chase, T.1    Schaw Jr., E.M.2
  • 25
    • 0020480240 scopus 로고
    • Thermodynamics and kinetics of single residue replacements in avian ovomucoid third domains: Effect on inhibitor interactions with serine proteinases
    • Empie, M.W.; Laskowski, M.Jr. Thermodynamics and kinetics of single residue replacements in avian ovomucoid third domains: effect on inhibitor interactions with serine proteinases. Biochemistry, 1982, 21, 2274-2284.
    • (1982) Biochemistry , vol.21 , pp. 2274-2284
    • Empie, M.W.1    Laskowski Jr., M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.