N-hydroxy peptides as substrates for α-chymotrypsin

Journal of Peptide Research

Volumn 54, Issue 6, 1999, Pages 544-548

  Bianco, Alberto ^a,b   Kaiser, D ^a   Jung, G ^a  

^a UNIVERSITY OF TÜBINGEN   (Germany)

^b INSTITUT DE BIOLOGIE MOLÉCULAIRE ET CELLULAIRE   (France)

Author keywords

chymotrypsin; Enzymatic degradation; N hydroxy peptides; Peptidomimetics; Substrates

Indexed keywords

CHYMOTRYPSIN A;

ARTICLE; CHEMICAL BOND; ENZYME DEGRADATION; HYDROGEN BOND; MOLECULAR INTERACTION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDE ANALYSIS; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; CATALYSIS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CHYMOTRYPSIN; HYDROLYSIS; PEPTIDES; SPECTRUM ANALYSIS; SUBSTRATE SPECIFICITY;

EID: 0032738396     PISSN: 1397002X     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3011.1999.00149.x     Document Type: Article

References (32)

1. Winkelmann, G. (1991) CRC Handbook of Microbial Iron Chelates. CRC Press, Boca Raton.
2. Drechsel, H. & Jung, G. (1998) Peptide siderophores. J. Pept. Sci. 4, 147-181.
3. Nishino, N. & Powers, J.C. (1979) Design of potent reversible inhibitors for thermolysin. Peptides containing zinc coordinating ligands and their use in affinity chromatography. Biochemistry 18, 4340-4347.
4. Bourdel, E., Doulut, S., Jarretou, G., Labbe-Jullie, C., Fehrentz, J.-A., Doumbia, O., Kitabgi, P. & Martinez, J. (1996) New hydroxamate inhibitors of neurotensin-degrading enzymes. Int. J. Pept. Protein Res. 48, 148-155.
5. Patel, D.V., Young, M.G., Robinson, S.P., Hunihan, L., Dean, B.J. & Gordon, E.M. (1996) Hydroxamic acid-based bisubstrate analog inhibitors of ras farnesyl protein transferase. J. Med. Chem. 39, 4197-4210.
6. Pickart, C.M. & Jencks, W.P. (1979) Formation of stable anhydrides CoA transferase and hydroxamic acids. J. Biol. Chem. 254, 9120-9129.
7. Dupont, V., Lecoq, A., Mangeot, J.-P., Aubry, A., Boussard, G. & Marraud, M. (1993) Conformational perturbations induced by N-amination and N-hydroxylation of peptides. J. Am. Chem. Soc. 115, 8898-8906.
8. Akiyama, M., Iesaki, K., Katoh, A. & Shimizu, K. (1986) N-Hydroxy amides. Part 5. Synthesis and properties of N-hydroxypeptides having leucine enkephaline sequences. J. Chem. Soc. Perkin Trans. 1, 851-855.
9. Takeuchi, Y. & Marshall, G.R. (1998) Conformational analysis of reverse-turn constraints by N-methylation and N-hydroxylation of amide bonds in peptides and non-peptide mimetics. J. Am. Chem. Soc. 120, 5363-5372.
10. Bracher, B.H. & Small, R.W.H. (1970) The crystal structure of acetohydroxamic acid hemihydrate. Acta Crystallogr. Sect. B 26, 1705-1709.
11. Smith, W.L. & Raymond, K.N. (1980) Synthesis of aliphatic dimeric N-isopropylhydroxamic acids and the crystal and molecular structure of N,N′-dihydroxy-N,N′-diisopropylhexanediamide: a hydroxamic acid in the trans conformation. J. Am. Chem. Soc. 102, 1252-1255.
12. Kolasa, T. (1983) The conformational behaviour of hydroxamic acids. Tetrahedron 39, 1753-1759.
13. Ottenheijm, H.C.J. & Herscheid, J.D.M. (1986) N-Hydroxy-α-amino acids in organic chemistry. Chem. Rev. 86, 697-707.
14. Hara, Y. & Akiyama, M. (1996) Peptide-based trihydroxamates as models for desferrioxamines. Iron (III)-holding properties of linear and cyclic N-hydroxy peptides with an L-alanyl-L-alanyl-N-hydroxy-β-alanyl sequence. Inorg. Chem. 35, 5173-5180.
15. Chen, J.J. & Spatola, A.F. (1997) Solid phase synthesis of peptide hydroxamic acids. Tetrahedron Lett. 38, 1511-1514.
16. Mellor, S.L., McGuire, C. & Chan, W.C. (1997) N-Fmoc-aminooxy-2-chlorotrityl polystyrene resin: a facile solid-phase methodology for the synthesis of hydroxamic acids. Tetrahedron Lett. 38, 3311-3314.
17. Bianco, A., Zabel, C., Walden, P. & Jung, G. (1998) N-Hydroxy-amide analogues of MHC-class 1 peptide ligands with nanomolar binding affinities. J. Pept. Sci. 4, 471-478.
18. Hin, S., Zabel, C., Bianco, A., Jung, G. & Walden, P. (1999) N-Hydroxy peptides: a new class of T cell receptor antagonists. J. Immunol. 163, in press.
19. Rötzschke, O., Falk, K., Stevanovic, S., Jung, G., Walden, P. & Rammensce, H.-G. (1991) Exact prediction of a natural T cell epitope. Eur. J. Immunol. 21, 2891-2894.
20. Jung, G. & Beck-Sickinger, A.G. (1992) Multiple peptide synthesis methods and their applications. Angew. Chem. Int., Ed. Engl. 31, 367-383.
21. Bax, A. & Davis, D.G. (1985) Practical aspects of two-dimensional transverse NOE spectroscopy. J. Magn. Res. 63, 207-213.
22. Bax, A. & Davis, D.G. (1985) MLEV-17-Based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Res. 65, 355-360.
23. Blow, M.D. (1976) Structure and mechanism of chymotrypsin. Acc. Chem. Res. 9, 145-152.
24. Ghosh, K.K., Rajput, S.K. & Krishnani, K. (1992) Kinetic model for acid-catalyzed hydrolysis of benzohydroxamic acid. J. Phys. Org. Chem. 5, 39-43.
25. Novak, M., Bonham, G.A., Mohler, L.K. & Peet, K.M. (1988) Acid-catalyzed hydrolysis of N-hydroxyacetanilide: amide hydrolysis vs N-O bond heterolysis. J. Org. Chem. 53, 3903-3908.
26. Di Furia, F., Modena, G. & Serimin, P. (1984) On the mechanism of acid catalyzed hydrolysis of hydroxamic acids. Nouv. J. Chim. 8, 45-49.
27. Warshel, A., Naray-Szabo, G., Sussman, F. & Hwang, J.-K. (1989) How do serine proteases really work? Biochemistry 28, 3629-3637.
28. Dutler, H. & Bizzozzero, S.A. (1989) Mechanism of the serine protease reaction. Stereoelectronic, structural, and kinetic considerations as guidelines to deduce reaction paths. Acc. Chem. Res. 22, 322-327.
29. Paetzel, M. & Dalbey, R.E. (1997) Catalytic hydroxyl/amine dyads within serine proteases. TIBS 22, 28-31.
30. Tulinsky, A. & Blevins, R.A. (1987) Structure of a tetrahedral transition state complex of α-chymotrypsin dimer at 1,8-Å resolution. J. Biol. Chem. 262, 7737-7743.
31. Kopple, K.D., Ohnishi, M. & Go, A. (1969) Conformations of cyclic peptides. IV. Nuclear magnetic resonance studies of cyclo-pentaglycyl-L-leucyl and cyclo-diglycyl-L-histidyl-diglycyl-L-tyrosyl. Biochemistry 8, 4087-4095.
32. Augspurger, J.D., Bindra, V.A., Scheraga, H.A. & Kuki, A. (1995) Helical stability of de novo designed α-aminoisobutyric acid-rich peptides at high temperatures. Biochemistry 34, 2566-2576.