It was found that tuftsin (Thr-Lys-Pro-Arg) and its tetrapeptide analo
gues with the same amino acid composition, but different sequences, de
monstrate immunosuppressive activity for the humoral, but not (excepti
ng 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 o
f peptides of the type investigated can seriously modulate their immun
obiological activities. We also found that tetrapeptides Thr-Arg-Lys-P
ro 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 displacem
ent of two basic amino acid residues.