Untitled

Abstract

Peptide Leu-Val-Cys-Tyr-Pro-Gln, identical to the bone marrow peptide MP-3, and its Val3 and Ser3 analogs, lacking SH-group, were synthesized by conventional methods of peptide chemistry in solution and, along with the MP-3 S-S-dimerization product, were studied with respect to their effect on the macrophage phagocytic activity. It was shown that the activity was only enhanced by peptide MP-3, which demonstrated the essential role of the SH-group in this function. The dimer analog of MP-3, unlike dimer analogs of other monocysteine-containing peptides, glutathione and HP5b, did not exhibit the inhibitory effect.

Spatial structure of myelopeptides: II. Conformational analysis of MP-4, MP-5, and MP-6

“…The bone marrow cells were found to produce a group of six low-molecular peptides (myelopeptides MP-1-MP-6), which are involved in immunoregulation and affect the progress of immune reactions of any kind [2][3][4][5][6]. Myelopeptides were shown to be species-nonspecific; i.e., they can successfully function in the cells of various animal species and humans.…”

“…Myelopeptides were shown to be species-nonspecific; i.e., they can successfully function in the cells of various animal species and humans. These peptides have recently been isolated, their primary structures were determined, and their analogues were chemically synthesized [5,6]. This allowed a thorough study of their properties and mechanism of action.…”