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Antibodies to the bovine prion protein were produced by immunizing mice of three lines with five synthetic fragments of the protein and six of their analogues. The analogues contained amino acid substitutions that, according to theoretical calculation, should lead to an increase in the immunogenic activity of peptides. All the peptides except for one induced the formation of antibodies. All the sera containing the antipeptide antibodies were tested by an immunohistochemical method. The sera effectively bound to brain preparations from an animal with spongiform encephalopathy were identified; it was shown that they do not interact with preparations of normal brain. Therefore, it was shown that the immunization of mice with synthetic fragments of a prion protein allows one to obtain specific antibodies suitable for the study and diagnostics of prion diseases. [ABSTRACT FROM AUTHOR]

Abstract Peptide fragments of conservative sites of PorA, OpaB, and NspA proteins of the outer membrane of serogroup B meningococci were synthesized. These peptides caused a pronounced protective effect in immunized mice infected with virulent homologous and heterologous strains of serogroups B and A meningococci. The protective effect appreciably increased, if the studied peptides were associated in a polycomponent preparation, which can be used in the construction of meningococcal bivalent B+A vaccine. [ABSTRACT FROM AUTHOR]

A water-soluble analogue F32 of the fusion peptide from influenza virus hemagglutinin was synthesized. It consisted of 32 aa residues and retained the ability to interact with lipid membranes; its N-terminal sequence 1–24 coincided with that of the fusion protein from hemagglutinin (strain A/PR/8/34), whereas residues 25–32 (GGGKKKKK) provided its solubility in water. The peptide induced the conductivity fluctuations in planar bilayer lipid membranes characteristic of active fusion peptides. Conditions were found using CD spectroscopy under which the structure of F32 inside detergent micelles, where it can be studied by high-resolution 1H NMR spectroscopy, is close to the structure of the peptide during its interaction with phospholipid liposomes. [ABSTRACT FROM AUTHOR]