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Volumn 49, Issue 24, 2010, Pages 4113-4116

Reversible and noncompetitive inhibition of β-tryptase by protein surface binding of tetravalent peptide ligands identified from a combinatorial split-mix library

Author keywords

Combinatorial chemistry; Enzymes; Inhibitors; Peptides; Supramolecular chemistry

Indexed keywords

ACTIVE SITE; COMBINATORIAL CHEMISTRY; COMBINATORIAL LIBRARY; INHIBITORS; NANOMOLAR AFFINITY; OLIGOPEPTIDES; PEPTIDE LIGAND; PROTEIN SURFACE; SERINE PROTEASE;

EID: 77953105398     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.200907221     Document Type: Article
Times cited : (20)

References (53)
  • 6
    • 65549127630 scopus 로고    scopus 로고
    • For some illustrative examples, see: a) J. A. Robinson, ChemBioChem 2009, 10, 971-973;
    • (2009) Chem Bio Chem , vol.10 , pp. 971-973
    • Robinson, J.A.1
  • 24
    • 33746310676 scopus 로고    scopus 로고
    • Angew. Chem. Int. Ed. 2006, 45, 4277-4281;
    • (2006) Angew. Chem. Int. Ed. , vol.45 , pp. 4277-4281
  • 40
    • 0027178826 scopus 로고
    • The wide pI range of tryptase results from the different degree of glycosylation of the enzyme: R. C. Benyon, J. A. Enciso, A. D. Befus, J. Immunol. 1993, 151, 2699-2706.
    • (1993) J. Immunol. , vol.151 , pp. 2699-2706
    • Benyon, R.C.1    Enciso, J.A.2    Befus, A.D.3
  • 41
    • 0026611749 scopus 로고
    • In the first position after the lysine scaffold, all library members carried glycine to introduce flexibility and achieve a certain length of the peptide arms. Additionally, glycine is known to reduce unwanted interchain aggregation within the peptide ligand: a) H. S. Marsden, A. M. Owsianka, S. Graham, G. W. McClean, C. A. Robertson, J. H. Subaksharpe, J. Immunol. Methods 1992, 147, 65-72;
    • (1992) J. Immunol. Methods , vol.147 , pp. 65-72
    • Marsden, H.S.1    Owsianka, A.M.2    Graham, S.3    McClean, G.W.4    Robertson, C.A.5    Subaksharpe, J.H.6
  • 44
    • 27844549490 scopus 로고    scopus 로고
    • Angew. Chem. Int. Ed. 2005, 44, 7208-7212.
    • (2005) Angew. Chem. Int. Ed. , vol.44 , pp. 7208-7212
  • 51
    • 70349556447 scopus 로고    scopus 로고
    • Under the conditions of the assay (25°C, < 1.0 min), enzymatic digestion of the studied inhibitors by either trypsin or chymotrypsin to any significant extent is unlikely, especially as branched-dendrimer-based peptides are cleaved much slower than linear peptides in general: P. Sommer, V. S. Fluxa, T. Darbre, J.-L. Reymond, ChemBioChem 2009, 10, 1527-1536.
    • (2009) Chem Bio Chem , vol.10 , pp. 1527-1536
    • Sommer, P.1    Fluxa, V.S.2    Darbre, T.3    Reymond, J.-L.4
  • 52
    • 0345268760 scopus 로고    scopus 로고
    • Commercially available heparin-free rhLung β-tryptase is stabilized by a high concentration of NaCl (2N). Even though the enzyme becomes inactive over time under standard assay conditions (100 mM NaCl), its enzymatic activity (ca. 1/3 of the activity of heparin-containing tryptase when freshly prepared) can be measured over the short timescale of the fluorescence assay: a) A. Lundequist, M. A. Juliano, L. Juliano, G. Pejler, Biochem. Pharmacol. 2003, 65, 1171 -1180;
    • (2003) Biochem. Pharmacol. , vol.65 , pp. 1171-1180
    • Lundequist, A.1    Juliano, M.A.2    Juliano, L.3    Pejler, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.