Wyniki wyszukiwania - BazTech

Ograniczanie wyników

4 Polish Journal of Chemistry

Znaleziono wyników: 4

Liczba wyników na stronie

Wyniki wyszukiwania

Wyszukiwano:
w słowach kluczowych: immunotropic activity

Sortuj według:

Ogranicz wyniki do:

New Analogues of Proline-Rich Protein Fragments : Synthesis and Their Effect on Resistance of Murine Thymocytes to Hydrocortisone

Wirkus-Romanowska I., Miecznikowska H., Janusz M., Szymaniec S., Fortuna W., Międzybrodzki R., Zablocka M., Lisowski J., Kupryszewski G.

Polish Journal of Chemistry

2000

Vol. 74, nr 7

979-984

New analogues of proline-rich protein (PRP) fragment were synthezed by the solid phase method using Boc/Bzl procedure. Dimer of the nonapeptide as well as dimer, trimer and tetramer of hexapeptide fragments of PRP possesing immunotropic activity were obtained.

Fragments of a Proline-Rich Polypeptide Settled on a Hexapeptide Carcass Constructed of Glycine and L-Lysine Residues : Synthesis and Biological Properties

Wirkus-Romanowska I., Miecznikowska H., Zablocka M., Rybka K., Fortuna W., Międzybrodzki R., Szymaniec S., Janusz M., Lisowski J., Kupryszewski G.

Polish Journal of Chemistry

2000

Vol. 74, nr 2

219-225

Proline-rich polypeptide fragments settled on a hexapeptide constructed od L-lysine and glycine residues were synthesized by the solid phase method: X-Lys(X)-Gly-Lys(X)-Gly-Lys(X)-Gly-OH, X= Tyr-Val-Pro-Leu-Phe-Pro and Y-Lys(Y)-Gly-Lys(Y)-Gly-Lys(Y)-Gly-OH, Y=Val-Glu-Ser-Tyr-Val-Pro-Leu-Phe-Pro. Imunotropic activity of the analogues was determined in a murine syste using resistance to hydrocortisone and in human cell cultures using induction of cytokines as indicators.

Cyclic Analogues of Proline-Rich Protein Fragments : part III. Synthesis of New Analogues, Conformational Studies and Evaluation of Immunotropic Activity

Wirkus-Romanowska I., Rodziewicz-Motowidło S., Miecznikowska H., Rolka K., Janusz M., Szymaniec S., Zabłocka A., Fortuna W.

Polish Journal of Chemistry

2000

Vol. 74, nr 8

1129-1141

The immunotropic activity of peptides studied evaluated in the murine system indicated that they are as active as the linear precursor in the resistance to hydrocortisone, but did not show activity in the human system. As reported previously, similar immunotropic profiles were observed in the case of two cyclic analogues. Superposition of most representative conformations of all four peptides in the fragment mentioned above (RMSD of A carbons is0.86 A) leads to the conclusion that this hexapeptide segment might be considered as bioactive.

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

Wirkus-Romanowska I., Ciurak M., Miecznikowska H., Rolka K., Janusz M., Szymaniec S., Krukowska K., Lisowski J., Kupryszewski G.

Polish Journal of Chemistry

1998

Vol. 72, nr 11

2394-2398

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.