Improvement of biological activity and proteolytic stability of peptides by coupling with a cyclic peptide

Bioorganic and Medicinal Chemistry Letters

Volumn 13, Issue 15, 2003, Pages 2583-2586

  Shibata, Kenji ^a   Suzawa, Toshiyuki ^a   Soga, Shiro ^a   Mizukami, Tamio ^a   Yamada, Koji ^a   Hanai, Nobuo ^a   Yamasaki, Motoo ^a  

^a KYOWA HAKKO KOGYO CO LTD   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ANTITHROMBOCYTIC AGENT; CYCLOPEPTIDE; ENDOTHELIN; FARNESYL TRANS TRANSFERASE; PEPTIDE; PROTEIN FARNESYLTRANSFERASE INHIBITOR; PROTEINASE; RAS PROTEIN; RECOMBINANT PROTEIN; RES 701 1; RES 701-1; TRANSFERASE;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; CELL ADHESION; CHEMISTRY; CONFORMATION; DRUG EFFECT; EXPERIMENTAL MELANOMA; GENETICS; METABOLISM; MOLECULAR GENETICS; MOUSE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN STABILITY; PROTEIN STRUCTURE; SYNTHESIS; THROMBOCYTE AGGREGATION; TUMOR CELL LINE;

EID: 0038309187     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-894X(03)00476-1     Document Type: Article

References (17)

1. Yamasaki M., Yano K., Yoshida M., Matsuda Y., Yamaguchi K.J. Antibiot. 47:1994;276.
2. Suzawa T., Shibata K., Tanaka T., Matsuda Y., Yamasaki M. Bioorg. Med. Chem. Lett. 7:1997;1715.
3. Shibata K., Suzawa T., Tanaka T., Matsuda Y., Yamasaki M. Bioorg. Med. Chem. 6:1998;2459.
4. Katahira R., Shibata K., Yamasaki M., Matsuda Y., Yoshida M. Bioorg. Med. Chem. 3:1995;1273.
5. Mills R.G., O'Donoghue S.I., Smith R., King G.F. Biochemistry. 31:1992;5640.
6. Contrary to our expectation, the peptide produced by coupling of 2 to RES-701-1 (11-16) showed much weaker ET receptor binding affinity than RES-701-1 of microbial origin. Because the 3D structure of RES-701-1 has proved to have an extraordinary 'lasso' structure, the tail part passes through the ring region, which is shown in ref 4 in details, a simple coupling of the ring to the tail could not reproduce that complex structure (see ref 7).
7. Katahira R., Shibata K., Yamasaki M., Matsuda Y., Yoshida M. Bioorg. Med. Chem. Lett. 5:1995;1595.
8. Pierschbacher M.D., Ruoslahti E. Proc. Natl. Acad. Sci. USA. 81:1984;5985.
9. Reiss Y., Stradley S.J., Gierasch L.M., Brown M.S., Goldstein J.L. Proc. Natl. Acad. Sci. USA. 88:1991;732.
10. Goldstein J.L., Brown M.S., Stradley S.J., Reiss Y., Gierasch L.M. J. Biol. Chem. 266:1991;15575.
11. Callahan J.F., Bean J.W., Burgess J.L., Eggleston D.S., Hwang S.M., Kopple K.D., Koster P.F., Nichols A., Peishoff C.E., Samanen J.M., Vasko J.A., Wong A., Huffman W.F. J. Med. Chem. 35:1992;3970.
12. Stradley S.J., Rizo J., Gierasch L.M. Biochemistry. 32:1993;12586.
13. Fields G.B., Noble R.L. Int. J. Peptide Protein Res. 35:1990;161.
14. Hara M., Akasaka K., Akinaga S., Okabe M., Nakano H., Gomez R., Wood D., Uh M., Tamanoi F. Proc. Natl. Acad. Sci. U. S. A. 90:1993;2281.
15. Adessi C., Soto C. Curr. Med. Chem. 9:2002;963.
16. Hruby V.J. Life Sci. 31:1982;189.
17. Olson G.L., Bolin D.R., Bonner M.P., Bos M., Cook C.M., Fry D.C., Graves B.J., Hatada M., Hill D.E., Kahn M., Madison V.S., Rusiecki V.K., Sarabu R., Sepinwall J., Vincent G.P., Voss M.E. J. Med. Chem. 36:1993;3039.