Abstract: Herein disclosed are bioactive peptides and proteins having immunomodulating and antiviral activity, more particularly histidine-rich bioactive peptide complexes having the following structural formula (SEQ ID NO: 29): wherein: X1 is preferably absent or is selected from among Gln, Ser, Asn, Val, Ala, Phe, and Asp, and R1 and R2 are peptide chains optionally contain the amino acid residues His and/or Cys that interact with transition metal ions. Whereas R1 is preferably selected from among His-Gly-Val-Ser-Gly(SEQ ID NO: 30), CysVal-Val-Thr-Gly- (SEQ ID NO: 31), Cys-Gly-, Val-Ser-Gly-, and His-Gly- or alternatively is absent, R2 is preferably selected from among -Val-His-Gly, -Val-Phe-Val, -Val-His, -Val-Asp or alternatively is absent. Such histidine-rich peptide complexes, primarily alloferon family peptides such as Alloferon-1 (SEQ ID NO: 1) with Zn ions, enable the creation of drugs with a targeted mechanism of action, and the design thereof with regard to understanding of drug target structure.

Abstract: The present invention refers to proteins and bioactive peptides with immunomodulating and antiviral activity. Present peptide complexes have three-dimensional structure and are described by the following structural formula (SEQ ID NO: 23): wherein: X1 is preferably absent or is selected from among Gln, Ser, Asn, Val, Ala, Phe, and Asp, and R1 and R2 are peptide chains containing the amino acid residues His or Cys that interact with transition metal ions, wherein R1 is preferably selected from among Cys-Val-Val-Thr-Gly- (SEQ ID NO: 31), Cys-Gly-, Val-Ser-Gly-, and His-Gly- or alternatively is absent and R2 is preferably selected from among -Val-His-Gly, -Val-Phe-Val, -Val-His, -Val-Asp or alternatively is absent. Such histidine-rich peptide complexes, primarily alloferon family peptides with Zn ions, enable the creation of drugs with a targeted mechanism of action, and the design thereof with regard to understanding of drug target structure.

Abstract: Herein disclosed are bioactive peptides and proteins having immunomodulating and antiviral activity, more particularly histidine-rich bioactive peptide complexes having the following structural formula (SEQ ID NO: 23): wherein: X1 is absent or contains not less than 1 amino acid and R1 and R2 are peptide chains containing the amino acid residues His or Cys, that interact with transition metal ions. Whereas R1 may contain up to 5 amino acid residues or alternatively be absent, R2 contains up to 3 amino acid residues or is alternatively absent. Such peptide complexes, primarily alloferon family peptides with Zn ions, enable the design of drugs based on an understanding of drug target structure and thus enable the creation of drugs with targeted mechanism of action.

Abstract: A vaccine having a fusion protein set forth as SEQ ID NO:1 containing antigenic determinants of haemagglutinins of influenza A and B viruses and flagellin fragments functioning as safe adjuvant, joined via flexible hinges is given, which can be used for prophylaxis of influenza caused by existing influenza A and B strains as well as by possible reassortants. Usage of the vaccine will provide a universal protection against influenza and provides safety, efficacy, polyvalence and preventive effect.

Abstract: The problem to be solved: absence of safe efficient universal vaccine against influenza. The solution: The vaccine based on the fusion protein consisting of antigenic determinants of haemagglutinins of influenza A and B viruses and flagellin fragments functioning as safe adjuvant (SEQ ID NO:1) joined via flexible hinges is given which can be used for prophylaxis of influenza caused by existing influenza A and B strains as well as by possible reassortants. Safety, efficacy, polyvalence and preventive effect have been demonstrated. Usage of the present vaccine will allow to provide a universal protection against influenza.

Abstract: The present invention refers to proteins and bioactive peptides with immunomodulating and antiviral activity. Present peptide complexes have three-dimensional structure and are described by the following structural formula (SEQ ID NO: 23): where: X1 is absent or contains not less than 1 amino acid; R1 and R2 peptide chains, containing amino acid residues, His or Cys, interactable with transition metal ions, with R1 containing up to 5 amino acid residues or absent; R2 contains up to 3 amino acid residues or absent. Histidine-rich peptide complexes, primarily alloferon family peptides with Zn ions, will make it possible to create drugs with targeted mechanism of action, and design them with regard to understanding of drug target structure.