[Ion channels of various types induced in lipid membranes by gramicidin A derivatives carrying a cationic sequence at their C-termini].

The channel-forming activity of gramicidin A derivatives carrying positively charged amino acid sequences at their C-termini was studied on planar bilayer lipid membranes and liposomes. We showed previously that, at low concentrations, these peptides form classical cation-selective pores typical of gramicidin A, whereas, at high concentrations, they form large nonselective pores. The ability of the peptides to form nonselective pores, which was determined by the efflux of carboxyfluorescein, an organic dye, from liposomes, decreased substantially as the length of the gramicidin fragment in the series of cationic analogues was truncated.

[Epitope of the catalytic subunit of viscumin, exposed on its interaction with a lipid bilayer].

It was previously shown that the catalytic subunit of the plant toxin viscumin induces aggregation of small unilamellar liposomes and this process is inhibited by the mab_TA7 monoclonal antibody produced to the denatured catalytic subunit of viscumin (Agapov, I.I. et al.

[Antigenic structure of the foot-and-mouth virus. VI. Functional segments of the immunodominant region of the VP1 protein of foot-and-mouth virus strains O1K and A22].

B- and T-epitopes have been localized within the protective fragments of VP1 protein, viz., 136-152 of the O1K strain and 135-159 of the A22 strain of the foot-and-mouth disease virus (FMDV). Antibodies eliciting after immunization of various animals with the 135-159 A22 peptide are directed to different sites of the peptide.

[Antigenic structure of the foot-and-mouth virus. V. Protection of naturally susceptible animals from foot-and-mouth disease using a synthetic peptide].

We have synthesized the peptide representing 135-159 VP1 sequence of A22 strain of the foot-and-mouth disease virus (FMDV). The synthetic peptide induced 100% protection of guinea pigs against the disease. Two-fold immunization of cuttle with the peptide and single immunization of sheep induced full protection of the animals against A22 strain of FMDV.