In order to study the importance of arginine residues 13 and 14 in apamin, the bee venom neurotoxin, four analogues, [Lys13]-apamin, [Lys14]-apamin, [Har4, Har13]-apamin and [Har4, har14]-apamin were synthesized and tested with respect to their neurotoxicity. The two lysine-apamins were prepared by the solid phase method on benzhydrylamine resins. Before oxidation to disulphides, the (S-Acm)4-peptides were isolated and characterized. Portions of the purified lysin peptides were converted to homoarginine analogues by guanidination. The four apamin analogues were lethal, but the lethal doses differed significantly. The results demonstrate that the arginine residue at position 14 is more important for the high toxicity than is the one at position 13. The circular dichroism (CD) spectrum of [Lys13]-apamin was identical with that of apamin itself, whereas the spectrum of [Lys14]-apamin showed certain deviations.