The mechanism of action of feG, an anti-inflammatory peptide, was explored using data mining, molecular modeling, and enzymatic techniques. The molecular coordinates of protein kinase A (PKA) were used to create six virtual isoforms of protein kinase C (PKCalpha, betaI, betaII, delta, iota, and zeta). With in silico techniques a binding site for feG was identified on PKCbetaI that correlated significantly with a biological activity, the inhibition of intestinal anaphylaxis. Since feG selectively increased the binding of a PKCbetaI antibody, it is proposed that this peptide inhibits the reassociation of the hydrophobic tail of PKCbetaI with its binding site and prevents the enzyme from assuming an inactive conformation.