Synthesis of bivalent inhibitors of eucaryotic proteasomes

Journal of Peptide Science

Volumn 6, Issue 1, 2000, Pages 36-46

  Loidl, Günther ^a   Musiol, Hans Jürgen ^a   Groll, Michael ^a   Huber, Robert ^a   Moroder, Luis ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

Bivalent inhibition; Pegylation; Peptide bis aldehydes; Proteasome; Synthetic inhibitors

Indexed keywords

ALDEHYDE DERIVATIVE; MACROGOL; MONOMER; OCTAPEPTIDE; PROTEASOME; PROTEASOME INHIBITOR; THREONINE;

ARTICLE; BINDING AFFINITY; DRUG POTENCY; ENZYME ACTIVE SITE; EUKARYOTE; NONHUMAN; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION;

CHYMASES; CHYMOTRYPSIN; CYSTEINE ENDOPEPTIDASES; ENZYME INHIBITORS; EUKARYOTIC CELLS; FUNGAL PROTEINS; INHIBITORY CONCENTRATION 50; MODELS, CHEMICAL; MULTIENZYME COMPLEXES; PEPTIDES; POLYETHYLENE GLYCOLS; PROTEASOME ENDOPEPTIDASE COMPLEX; SACCHAROMYCES CEREVISIAE; SERINE ENDOPEPTIDASES; TRYPSIN; TRYPTASES;

EUKARYOTA;

EID: 0033956214     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1099-1387(200001)6:1<36::AID-PSC232>3.0.CO;2-2     Document Type: Article

References (32)

1. Groettrup M, Schmidtke G. Selective proteasome inhibitors: modulators of antigen presentation? DDT 1999; 4: 63-71.
2. Groll M, Ditzel L, Löwe J, Stock D, Bochtler M, Bartunik HD, Huber R. Structure of 20S proteasome from yeast at 2.4 Å resolution. Nature 1997; 386: 463-471.
3. Heinemeyer W, Fischer M, Krimmer T, Stachon U, Wolf DH. The active sites of the eukaryotic 20 S proteasome and their involvement in subunit precursor processing. J. Biol. Chem. 1997; 272: 25200-25209.
4. Nussbaum AK, Dick TP, Keilholz W, Schirle M, Stevanovic S, Dietz K, Heinemeyer W, Groll M, Wolf DH, Huber R, Rammensee H-G, Schild H. Cleavage motifs of the yeast 20S proteasome β subunits deduced from digests of enolase I. Proc. Natl. Acad. Sci. USA 1998; 95: 12504-12509.
5. Arendt CS, Hochstrasser M. Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation. Proc. Natl. Acad. Sci. USA 1997; 94: 7156-7161.
6. Dick LR, Aldrich C, Jameson SC, Moomaw CR, Pramanik BC, Doyle CK, DeMartino GN, Bevan MJ, Forman JM, Slaughter CA. Proteolytic processing of ovalbumin and β-galactosidase by the proteasome to yield antigenic peptides. Immunology 1994; 152: 3884-3894.
7. Ehring B, Meyer TH, Eckerskorn C, Lottspeich F, Tampé R. Effects of major-histocompatibility-encoded subunits on the peptidase and proteolytic activites of human 20S proteasomes. Eur. J. Biochem. 1996; 235: 404-415.
8. Kuckelkorn U, Frentzel S, Kraft R, Kostka S, Groettrup M, Kloetzel P-M. Incorporation of major histocompatibility complex-encoded subunits LMP2 and LMP7 changes the quality of the 20S proteasome polypeptide processing products independent of interferon-γ. Eur. J. Immunol. 1995; 25: 2605-2611.
9. Niedermann G, King G, Butz S, Birsner U, Grimm R, Shabanowitz J, Hunt DF, Eichmann K. The proteolytic fragments generated by vertebrate proteasomes: structural relationships to major histocompatibility complex I binding peptides. Proc. Natl. Acad. Sci. USA 1996; 93: 8572-8577.
10. Ossendorp F, Eggers M, Neisig A, Ruppert T, Groettrup T, Sijts A, Mengede E, Kloetzel P-M, Neefjes J, Koszinowski U, Melief C. A single residue exchange within a viral CTL epitope alters proteasome-mediated degradation resulting in lack of antigen presentation. Immunity 1996; 5: 115-124.
11. Fenteany G, Standaert RF, Lane WS, Choi S, Corey EJ, Schreiber SL. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 1995; 268: 726-731.
12. Dick LR, Cruikshank AA, Destree AT, Grenier L, McCormack TA, Melandri FD, Nunes SL, Palombella VJ, Parent LA, Plamondon L, Stein RL. Mechanistic studies on the inactivation of the proteasome by lactacystin in cultured cells. J. Biol. Chem. 1997; 272: 182-188.
13. Corey EJ, Reichard GA, Kania R. Studies on the total synthesis of lactacystin: an improved aldol coupling reaction and a beta-lactone intermediate in thiol ester formation. Tetrahedron Lett. 1993; 34: 6977-6980.
14. Ostrowska H, Woijcik C, Omura S, Worowski K. Lactacystin, a specific inhibitor of the proteasome, inhibits human platelet lysosomal cathepsin A-like enzyme. Biochem. Biophys. Res. Comm. 1997; 234: 729-732.
15. Bogyo M, McMaster JS, Gaczynska M, Tortorella D, Goldberg AL, Ploegh H. Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HsIV by a new class of Inhibitors. Proc. Natl. Acad. Sci. USA 1997; 90: 6629-6634.
16. Bogyo M, Shin S, McMaster JS, Ploegh H. Substrate binding and sequence preference of the proteasome revealed by active-site-directed affinity probes. Chem. Biol. 1998; 5: 307-320.
17. Spaltenstein A, Leban JJ, Huang JJ, Reinhardt KR, Viveros OH, Sigafoos J, Crouch R. Design and synthesis of novel protease inhibitors. Tripeptlde α',β'-epoxyketones as nanomolar inactivators of the proteasome. Tetrahedron Lett. 1996; 37: 1343-1346.
18. Meng L, Kwok BH, Sin N, Crews CM. Eponemycin exerts its antitumor effect through the inhibition of proteasome function. Cancer Res. 1999; 59: 2798-2801.
19. Adams J, Behnke M, Chen S, Cruickshank AA, Dick LR, Grenier L, Klunder JM, Ma Y-T, Plamondon L, Stein RL. Potent and selective inhibitors of the proteasome: dipeptidyl boronic acids. Bioorg. Med. Chem. Lett. 1998; 8: 333-338.
20. Pereira PJB, Bergner A, Macedo-Ribeiro S, Huber R, Matschiner G, Fritz H, Sommerhoff CP, Bode W. Human beta-tryptase in a ring-like tetramer with active sites facing a central pore. Nature 1998; 392: 306-311.
21. Page MI, Jencks WP. Entropie contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect. Proc. Natl. Acad. Sci. USA 1971: 68: 1678-1683.
22. Spike CG, Parry RW. Thermodynamics of chelation. I. The statistical factor in chelate ring formation. J. Am. Chem. Soc. 1953: 75: 2726-2729.
23. Crothers DM, Metzger H. The influence of polyvalency on the binding properties of antibodies. Immunochemistry 1972; 9: 341-357.
24. Mammen M, Choi S-K, Whitesides GM. Polyvalent interactions in biological systems - Implications for design and use of multivalent ligands and inhibitors. Angew. Chem. Int. Ed. Engl. 1998; 37: 2755-2794.
25. Loidl G, Groll M, Musiol H-J, Huber R, Moroder L. Bivalency as a principle of proteasome inhibition. Proc. Natl. Acad. Sci. USA 1999; 96: 5418-5422.
26. Loidi G, Musiol H-J, Groll M, Ditzel L, Huber R, Moroder L. Bivalent inhibitors of the yeast proteasome. In Peptides 1998, Bajusz S, Hudecz F (eds). Budapest: Akademiai Kiadó, 1999; 828-829.
27. Schaschke N, Musiol H-J, Assfalg-Machleidt I, Machleidt W, Rudolph-Bohner S, Moroder L. Cyclodextrins as templates for the presentation of protease inhibitors. FEBS Lett. 1996; 391: 297-301.
28. Loidl G, Groll M, Muslol H-J, Ditzel L, Huber R, Moroder L. Bifunctional inhibitors of the trypsin-like activity of eukaryoticproteasomes. Chem. Biol. 1999; 6: 197-204.
29. Ditzel L, Huber R, Mann K, Heinemeyer W, Wolf DH, Groll M. Conformational constraints for protein self-cleavage in the proteasome. J. Mol. Biol. 1998; 279: 1187-1191.
30. Kisselev AF, Akopian TN, Woo KM, Goldberg AL. The sizes of peptides generated from protein by mammalian 26 and 20S proteasome. J. Biol. Chem. 1999; 274: 3363-3371.
31. Harris JM (ed.) Poly(ethylene glycol) Chemistry, Plenum: New York.
32. Burgess LE, Newhouse BJ, Ibrahim P, Rizzi J, Kashem MA, Hartmann A, Brandhuber BJ, Wright CD, Thomson DS, Vigers GPA, Koch K. Potent selective nonpeptidic inhibitors of human lung tryptase. Proc. Natl. Acad. Sci. USA 1999; 96: 8348-8352.