A new class of sequential oligopeptide carriers (SOC n ), namely (Lys-Aib-Gly) n (n = 2-7), for anchoring antigenic peptides, is presented. These SOC n have been designed in order to assume a determined structural motif, exhibiting defined spatial orientations of the Lys-N H 2 anchoring groups. The NMR study showed that SOC n adopt a rigid conformation with some regularity, initiated from the C-terminus of the carrier, while molecular dynamics simulation confirmed the occurrence of a distorted 3 1 0 -helix. It was also demonstrated, by 1 HNMR, that all the antigenic peptides bound to the SOC n retain their original, folded active, structure and that probably they do not interact to each other. It is concluded that the beneficial structural elements of the SOC n impose a favorable disposition of the anchored peptides so that potent antigens with maximum molecular recognition are generated.