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EN
The cyclic hexadecapeptide containing human heat shock protein 70(29-42) fragment cyclized by the disulfide bridge between two L-cysteine residues introduced at the N- and C-termini was synthesized by the solid phase method. It was established that the cyclic analogue, contrary to its linear counterpart, had much lower ability to generate immune response in rabbits. Conformational studies of cyclic peptide performed using 1D and 2D 1H-NMR spectroscopy in conjunction with theoretical conformational analysis revealed that the cyclization constrained the 3D structure of this peptide, reflected by the observed rate of cis/trans isomerization of Arg9-Thr10 peptide bond and the presence of Gly7-Asn8 peptide bond in cis geometry.We, therefore, postulate that the conformational flexibility in the case of Human Heat Shock Protein fragments is a key element for their immunogenicity.
EN
Three polypetide fragments of hepatitis C virus protein were synthesized using the solid-phase method. The immunogenicity of the peptides was tested. All the peptides exhibit immunological activity.
EN
The 29-42 fragment of human heat shock protein 70 (hsp 70) was synthesized by the solid phase method. As determined by enzyme-linked immunosorbent assay (ELISA), the synthetic hsp 70(29-42) peptide generated relatively strong immune response in immunized rabbits. Antibody titers were comparable with anti hsp 70 antibody serum level that was induced by immunization with recombinant protein (hsp 70). It was established that antibodies directed against hsp 70(29-42) peptide could be applied in ELISA for detecting hsp 70 in body fluids and tissues.
EN
Three polypeptide fragments of Hepatitis C virus protein (130-140)C, (133-142)C and (1406-1415)NS3 were synthesized using the solid-phase method. The immunogenicity of the peptides was tested on rabbits. All the peptides studied revealed homoral and cell response.
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