Proteolytically stable peptides by incorporation of α-Tfm amino acids

Journal of Peptide Science

Volumn 3, Issue 3, 1997, Pages 157-167

  Koksch, Beate ^a   Sewald, Norbert ^a   Hofmann, Hans Jörg ^a   Burger, Klaus ^a   Jakubke, Hans Dieter ^a  

^a UNIVERSITY OF LEIPZIG   (Germany)

Author keywords

C , disubstituted glycines; Proteolytic stability; chymotrypsln; Trifluoromethyl substituted amino acids

Indexed keywords

2 AMINO 2 METHYLPROPIONIC ACID; 2-AMINOISOBUTYRIC ACID; CHYMOTRYPSIN; DIMETHYL SULFOXIDE; FLUORINE; PEPTIDE;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; METHODOLOGY; METHYLATION; PROTEIN ENGINEERING; SYNTHESIS;

AMINOISOBUTYRIC ACIDS; CHYMOTRYPSIN; DIMETHYL SULFOXIDE; FLUORINE; METHYLATION; MODELS, MOLECULAR; PEPTIDES; PROTEIN ENGINEERING;

EID: 0031132903     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1099-1387(199705)3:3<157::aid-psc94>3.0.co;2-w     Document Type: Article

References (25)

1. G. Hölzemann (1991). Peptide conformation mimetics (Part 1). Kontakte (Darmstadt) 1, 3-12.
2. S. M. Miller, R. J. Simon, S. Ng, R. N. Zuckermann, J. M. Kerr and W. H. Moos (1994). Proteolytic studies of homologous peptide and N-substituted glycine peptoid oligomers. Bioorg. Med. Chem. Lett. 4, 2657-2662.
3. S. A. Gillmor and F. E. Cohen (1993). New strategies for pharmaceutical design. Receptor 3, 155-163.
4. J. Rizo and L. M. Gierasch (1992). Constrained peptides: Models of bioactive peptides and protein substructures. Ann. Rev. Biochem. 61, 387-418.
5. α,α-disubstituted glycines. Int. J. Peptide Protein Res. 37, 521-527.
6. 10-helices. Int. J. Peptide Protein Res. 44, 539-548.
7. K.-H. Altmann, E. Altmann and M. Mutter (1992). Conformational studies on peptides containing enantiomeric α-methyl α-amino acids. Part I. Differential Conformational properties of (R)- and (S)-2-methyl-aspartic acid. Helv. Chim. Acta 75, 1198-1210.
8. V. Matha, A. Jegorov, M. Kiess and H. Brückner (1992). Morphological alterations accompanying the effect of peptaibiotics, α-aminoisobutyric acid-rich secondary metabolites of filamentous fungi, on Culex pipiens larvae. Tissue Cell 24, 559-564.
9. α-benzylglycine [(αMe)Phe] model peptides. Peptide Res. 5, 56-61.
10. N. Sewald and K. Burger in: Fluorine-containing Amino Acids, Synthesis and Properties, V. P. Kukhar, V. A. Soloshonok, Eds., p. 139-220, Wiley, Chichester 1995, and references therein.
11. K. Burger, K. Mütze, W. Hollweck, B. Koksch, P. Kuhl, H.-D. Jakubke, J. Riede and A. Schier (1993). Untersuchungen zur proteasekatalysierten und chemischen Peptidbindungsknüpfung mit α-trifluormethylsubstituierten α-Aminosäuren. J. Prakt. Chem./Chem.-Ztg. 335, 321-331.
12. D. Seebach (1990). Organic synthesis - where next? Angew. Chem., Int. Ed. Engl. 29, 1320-1367.
13. T. Nagai, G. Nishioka, M. Koyama, A. Ando, T. Miki and I. Kumadaki (1992). Reactions of trifluoromethyl ketones. IX. Investigation of the steric effect of a trifluoromethyl group based on the stereochemistry on the dehydration of trifluoromethyl homoallyl alcohols. J. Fluorine Chem. 57, 229-237.
14. K. Möhle and H.-J. Hofmann (1995). Conformational studies on peptides with unusual amino acid side-chains: The trifluoromethyl group. J. Mol. Structure (Theochem.) 339, 57-65.
15. A. R. Fersht: Enzyme Structure and Mechanism, Freeman, New York 1985.
16. K. Burger, E. Höß, K. Gaa, N. Sewald and Ch. Schierlinger (1991). New synthetic pathways to 3,3,3-trifluoroalanine, 2-deutero-3,3,3-trifluoroalanine and their derivatives. Z. Naturforsch. 46b, 361-384.
17. N. Sewald, W. Hollweck, K. Mütze, C. Schierlinger, L. C. Seymour, K. Gaa, K. Burger, B. Koksch and H. D. Jakubke (1995). Peptide modification by introduction of α-trifluoromethyl substituted amino acids. Amino Acids 8, 187-194.
18. B. Koksch, PhD Thesis, University of Leipzig 1995.
19. Ch. Schierlinger and K. Burger (1992). Peptide modification by α-trifluoro-methyl α-amino acids via 4-trifluoromethyl-1,3-oxazolidin-2,5-diones. Tetrahedron Lett. 33, 193-194.
20. QUANTA 4.1., Molecular Simulation Inc., Burlington, MA 1994.
21. V. Schellenberger, U. Schellenberger, Y. V. Mitin and H.-D. Jakubke (1990). Characterization of the S′-subsite specificity of bovine pancreatic α-chymotrypsin via acyl transfer to added nucleophiles. Eur. J. Biochem. 187, 163-167.
22. I. Schechter and A. Berger (1967). On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27, 157-162.
23. M. I. Vidal, M. L. M. Serralheiro and J. M. S. Cabral (1992). Thermostability of α-chymotrypsin in water/organic solvent systems. Biotechnol. Lett. 14, 1041-1044.
24. A. Tulinsky and R. A. Blevins (1987). Structure of a tetrahedral transition state complex of alpha-chymotrypsin at 1.8 Å resolution. J. Biol. Chem. 262, 7737.
25. H. Dutler and S. Bizzozero (1989). Mechanism of the serine protease reaction. Stereoelectronic, structural, and kinetic considerations as guidelines to deduce reaction paths. Acc. Chem. Res. 22, 322-327.