Cyclic analogues of proline-rich protein fragments. Part 1. Synthesis and evaluation of immunotropic activity

• Autorzy: Wirkus-Romanowska I. , Ciurak M. , Miecznikowska H. , Rolka K. , Janusz M. , Szymaniec S. , Krukowska K. , Lisowski J. , Kupryszewski G.
• Języki publikacji: EN

Abstrakty

EN

Proline-rich protein (PRP), isolated from ovine colostrum, possesses strong immunotropic activity. The nonapeptide (Val-Glu-Ser-Tyr-Val-Pro-Leu-Phe-Pro) and the hexapeptide (Tyr-Val-Pro-Leu-Phe-Pro) PRP fragments reveled biological activity similar to that of the native protein. Seeking for analogues of PRP fragments with costrained structure, two cyclic peptides were synthesized by the solid phase method: Cys-Val-Glu-Ser-Tyr-Val-Pro-Leu-Phe-Pro-Cys and Ac-Glu-Tyr-Val-Pro-Leu-Phe-Pro-Lys-NH2. Immunotropic activity of both peptides in murine system was the same as for linear nonapeptide, whereas all three peptides were practically inactive in human system, where resistance to hydrocortisone and induction of two cytokinins IFN and TNF were used as indicators, respectively.

Słowa kluczowe

EN

cyclic PRP fragments; solid phase peptide synthesis; immunotropic activity

• Wydawca: Polskie Towarzystwo Chemiczne
• Czasopismo: Polish Journal of Chemistry
• Rocznik: 1998
• Tom: Vol. 72, nr 11
• Strony: 2394--2398
• Opis fizyczny: Bibliogr. 19 poz., tab.

Twórcy

autor

Wirkus-Romanowska I.

autor

Ciurak M.

autor

Miecznikowska H.

autor

Rolka K.

autor

Janusz M.

autor

Szymaniec S.

autor

Krukowska K.

autor

Lisowski J.

autor

Kupryszewski G.

• Faculty of Chemistry, University of Gdańsk, ul. Sobieskiego 18 80-952 Gdańsk, Poland