Design of serine proteinase inhibitors by combinatorial chemistry using trypsin inhibitor SFTI-1 as a starting structure

Journal of Peptide Science

Volumn 13, Issue 11, 2007, Pages 749-755

  Zabłotna, Ewa ^a   Jaśkiewicz, Anna ^a   Łegowska, Anna ^a   Miecznikowska, Hanna ^a   Lesner, Adam ^a   Rolka, Krzysztof ^a  

^a UNIVERSITY OF GDA SK   (Poland)

Author keywords

Chymotrypsin; Combinatorial chemistry; Elastase; Inhibitors; Serine proteinases; Trypsin

Indexed keywords

9 FLUORENYLMETHYL CHLOROFORMATE; AMINO ACID; ARGININE; BOWMAN BIRK INHIBITOR; CHYMOTRYPSIN INHIBITOR; ELASTASE INHIBITOR; LEUCINE; METHIONINE; PEPTIDE LIBRARY; PHENYLALANINE; PLANT EXTRACT; PROLINE; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR; SFTI 1; SUNFLOWER EXTRACT; TRYPSIN; TRYPSIN INHIBITOR; UNCLASSIFIED DRUG;

COMBINATORIAL CHEMISTRY; CONFERENCE PAPER; DRUG DESIGN; DRUG POTENCY; DRUG SYNTHESIS; ENZYME INHIBITION; EQUILIBRIUM CONSTANT; NONHUMAN; PEPTIDE SYNTHESIS; PLANT SEED; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN MODIFICATION; SOLID PHASE SYNTHESIS; SUNFLOWER;

AMINO ACID SEQUENCE; ANIMALS; CATTLE; CHYMOTRYPSIN; HUMANS; LEUKOCYTE ELASTASE; MOLECULAR SEQUENCE DATA; PEPTIDE LIBRARY; PEPTIDES, CYCLIC; PLANT PROTEINS; SERINE PROTEINASE INHIBITORS; TRYPSIN INHIBITORS;

HELIANTHUS;

EID: 36049048887     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.887     Document Type: Conference Paper

References (23)

1. Laskowski M, Quasim MA Jr. What can the structures of enzyme-inhibitor complexes tell us about the structures of enzyme substrate complexes? Biochem. Biophys. Acta 2000; 1477: 324-337.
2. Bode W, Huber R. Natural protein proteinase inhibitors and their interaction with proteinases. Eur. J. Biochem. 1992; 204: 433-451.
3. Luckett S, Santiago Garcia R, Barker JJ, Konarev AV, Shewry PR, Clarke AR, Brady RL. High-resolution structure of a potent, cyclic proteinase inhibitor from sunflower seeds. J. Mol. Biol. 1999; 290: 525-533. i
4. 1H NMR of the novel cyclic trypsin inhibitor SFTI-1 from sunflower seeds and an acyclic permutant. J. Mol. Biol. 2001; 311: 579-591.
5. Korsinczky MLJ, Schirra HJ, Craik DJ. Sunflower trypsin inhibitor-l. Curr. Protein Pept. Sci. 2004; 5: 351-364.
6. McBride JD, Watson EM, Brauer ABE, Jaulent AM, Leatherbarrow RJ. Peptide mimics of the Bowman-Birk inhibitor reactive site loop. Biopolymers 2002; 66: 79-92. i
7. Qi RF, Song ZW, Chi CW. Structural features and molecular evolution of Bowman-Birk protease inhibitors and their potential application. Acta Biochem. Biophys. Sin 2005; 37: 283-292.
8. Zabłotna E, KaYmierczak K, Jaokiewicz 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.
9. 1 reactive site. ChemBioChem 2005; 6: 107-1061.
10. 1 position of trypsin inhibitor SFTI-1 from sunflower seeds retains its activity. Biochem. Biophys. Res. Commun. 2006; 340: 823-828.
11. Descours A, Moehle K, Renard A, Robinson JA. A new family of beta-hairpin mimetics based on a trypsin inhibitor from sunflower seeds. ChemBioChem 2002; 3: 318-323.
12. Brauer ABE, Domingo GJ, Cooke RM, Matthews SJ, Leatherbarrow RJ. A conserved cis peptide bond is necessary for the activity of Bowman-Birk inhibitor protein. Biochemistry 2002; 41: 10608-10615.
13. Hilpert K, Hansen G, Wessner H, Volkmer-Engert R, Höhne W. Complete substitutional analysis of a sunflower trypsin inhibitor with different serine proteases. J. Biochem. 2005; 138: 383-390.
14. KaYmierczak K, Zabłotna E, Jaokiewicz A, Miecznikowska H, Rolka K. Selection of low-molecular mass trypsin and chymotrypsin inhibitors based on the binding loop of CMTI-III using combinatorial chemistry approach. Biochem. Biophys. Res. Commun. 2003; 310: 811-815.
15. Sole NA, Barany G. Optimization of solid-phase synthesis of (8-A1a)-dynorphin A. J. Org. Chem. 1992; 57: 5399-5403.
16. Stewart JM, Young JD. In Solid-Phase Peptide Synthests, 2nd ed. Pierce Chemical: Rockford, 1984; 95.
17. Empie MW, Laskowski M Jr. Thermodynamics and kinetics of single residue replacements in avian ovomucold third domains: effect on inhibitor interactions with serine proteinases. Biochemistry 1982; 21: 2274-2284.
18. Park SJ. Effect of amino acid replacements in ovomucoid third domains upon their association with serine proteinases. In PhD thesis, Purdue University, West Lafayette, 1985.
19. Marquardt DW. An algorithm for least-squares estimation of nonlinear parameters. J. Soc. Indust. Appl. Math 1963; 11: 431-441.
20. 189 in the substrate pocket of trypsin has an essential influence on the inhibitory activity. Biochem. Biophys. Res. Commun. 1997; 240: 869-871.
21. 1 variants of bovine pancereatic trypsin inhibitor to four serine proteases. J. Mol. Biol. 1999; 289: 175-186.
22. McBride JD, Freeman N, Domingo GJ, Leatherbarrow RJ. Selection of chymotrypsin inhibitors from a conformationally-constrained combinatorial peptide library. J. Mol. Biol. 1996; 259: 819-827.
23. McBride JD, Freeman HNM, Leatherbarrow RJ. Election of human elastase inhibitors from a conformationally constrained combinatorial peptide library. Eur. J. Biochem. 1999; 266: 403-412.