title: The immunomodulatory activity of tetra- and tripeptides of tuftsin-kentsin group.
abstract: It was found that tuftsin (Thr-Lys-Pro-Arg) and its tetrapeptide analogues with the same amino acid composition, but different sequences, demonstrate immunosuppressive activity for the humoral, but not (excepting the Thr-Lys-Arg-Pro tetrapeptide) for the cellular, immune response. The splitting of N-terminal residues from these tetrapeptides leads, however, to formation of tripeptides that are active in both humoral and cellular immune response tests. Thus, the biological degradation of peptides of the type investigated can seriously modulate their immunobiological activities. We also found that tetrapeptides Thr-Arg-Lys-Pro and Thr-Lys-Arg-Pro, as well as tripeptides Arg-Lys-Pro and Lys-Arg-Pro, distinctly differ in their immunomodulatory activities, although the structural differences consist in this case only in the displacement of two basic amino acid residues.
authors.affiliation: Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wrocław.
authors.forename: Z
authors.initials: Z
authors.lastname: Wieczorek
authors.forename: M
authors.initials: M
authors.lastname: Zimecki
authors.forename: J J
authors.initials: JJ
authors.lastname: Słoń
authors.forename: I Z
authors.initials: IZ
authors.lastname: Siemion
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000917:Antibody Formation / Q000187:drug effects*; D006968:Hypersensitivity, Delayed; D007111:Immunity, Cellular / Q000187:drug effects; D007166:Immunosuppressive Agents / Q000494:pharmacology*; D051379:Mice; D008808:Mice, Inbred CBA; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000494:pharmacology*; D012397:Rosette Formation; D013154:Spleen / Q000166:cytology / Q000276:immunology; D014405:Tuftsin / Q000031:analogs & derivatives* / Q000494:pharmacology*
chemical_list: D007166:Immunosuppressive Agents; D009842:Oligopeptides; C017147:kentsin; D014405:Tuftsin