[Synthesis of stearoyl derivatives of proline-containing hydrophobic peptides].

Hydrophobic stearoyl derivatives of proline-containing di- and tripeptides and their deuterated analogs were synthesized. It was shown by NMR spectroscopy that cis-trans-equilibrium around an X-Pro peptide bond is displaced towards trans-conformers for compounds containing a Ste-Pro fragment as opposed to the compounds containing Boc-Pro or Gly-Pro fragments.

[Protein motifs and their structure-functional role].

The review deals with repeating fragments of amino acid sequences, so-called "motifs", that are important in maintaining structural integrity and/or function of various proteins, especially those interacting with phospholipid aggregates. The occurrence of Phe-Leu-Gly motif characteristic for the amino acid sequence of the primate immuno-deficiency viruses fusion peptides is analysed in various proteins, as well as tripeptide fragments of general formula Xaa-Xah-Gly (Xaa-Phe, Tyr; Xab-hydrophobic amino acids Ala, Val, Leu, Ile) homologous to the above motif and retro-sequences Gly-Xab-Xaa. These tripeptide repeats are characteristic for the amino acid sequences of complex membrane proteins, viral envelope proteins, proteinases and proteins connected with energy transfer or interacting with lipids.

[Synthesis of the tripeptide glycyl-L-leucyl-L-phenylalanine and its analogs].

Peptide Gly-L-Leu-L-Phe and its derivatives were synthesized by the C-end elongation utilizing DCC/HOBT technique and by enzymatic route with the help of papain using esters of N-benzyloxycarbonyl-glycine and -L-leucine as acyl donors have been suggested. The chemical, similarly to the enzymatic, synthesis was not accompanied by racemization. Conditions for HPLC separation and preparative isolation of the enzymatic reaction products were developed.