Four analogs of the natural macrophage-activator peptide tuftsin (T-K-
P-R) were synthesized with the aim of obtaining compounds more effecti
ve in the stimulation of the immune system than tuftsin. Modifications
to the parent tuftsin molecule were (i) substitution of the proline (
P) residue, and/or (ii) replacement of the N-terminal residue threonin
e (T). The study presented here shows that the integrity of the NH2 te
rminus is not mandatory for a full biological tuftsin-like activity. O
ur data also suggest that the analogue F-(psi)-K-ABO-R, where ABO is a
non-natural amino acid, is a promising agent for immunotherapy of inf
ectious and neoplasic diseases for which tuftsin has already demonstra
ted some efficacy.