Tytuł artykułu
Autorzy
Identyfikatory
Warianty tytułu
Języki publikacji
Abstrakty
The object of these investigations was synthesis and biological evaluation of new analogues of proctolin (H-Arg-Tyr-Leu-Pro-Thr-OH) modified at position 4 of the peptide chain by natural or non-natural amino acid residues, such as: Phe (1), D-Phe (2), Phg (3), D-Phg (4), N-Me-Ala (5), N-Me-Val (6), N-Me-Leu (7), Tyr (8), Arg (9), Lys (10), Nva (11), Acp (12), Ser (13), _-Abu (14), and _3,4-Pro (15). Synthesis was performed by classical solid-phase method. Myotropic activity of proctolin analogues was assayed in vitro on the semi-isolated heart of the yellow mealworm Tenebrio molitor. Analogues 1,9, and 14 retained about 50% of proctolin activity. Other analogues showed about 20% activity or were inactive. The importance of the hydrophobic amino acid residues at position 4 for the myotropic activity of proctolin was inferred.
Wydawca
Czasopismo
Rocznik
Tom
Strony
423--430
Opis fizyczny
Bibliogr. 5 poz., rys.
Twórcy
autor
- Faculty of Chemistry, University of Wrocław, PL 50-383 Wrocław, ul. F. Joliot-Curie 14, Poland
autor
- Department of Animal Physiology, A. Mickiewicz University, 60-225 Poznań, Poland
autor
- Faculty of Chemistry, University of Wrocław, PL 50-383 Wrocław, ul. F. Joliot-Curie 14, Poland
Bibliografia
- 1. Konopińska D., J. Peptide Res., 49, 457 (1997).
- 2. Konopińska D. and Rosiński G., J. Peptide Sci., 5, 533 (1999).
- 3. Konopińska D., Bartosz-Bechowski H., Rosiński G. and Sobotka W., Bull. Pol. Acad. Sci. Chem., 41 (1993).
- 4. Kuczer M., Rosiński G., Lisowski M., Picur B. and Konopińska D., Int. J. Peptide Protein Res., 48, (1996).
- 5. Rosiński G. and Gade G., J. Insect Physiol., 33, 451 (1988).
Typ dokumentu
Bibliografia
Identyfikator YADDA
bwmeta1.element.baztech-article-BUJ1-0023-0188