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EN
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.
EN
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.
EN
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.
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