Several peptide mimics of a conserved H5N1 avian influenza virus neutralization site recognized by 8H5 mAb have been reported previously. In this study, the secondary and possibly higher structural orders of the peptide mimics 122 and 125 were investigated and found to be closely related to the specific binding with 8H5 mAb. These two peptide mimics were fused to three different carrier proteins, and the antibody binding activities were recovered in 4 of the 11 fusion proteins. HEV structural protein p239 and HBc were more suitable than the outer membrane protein T47 of the Treponema pallidum particle for the recovery of reactivity. The increase in the copy number of peptide mimics was important for the recovery of antibody-binding activity and the interaction between peptide and carrier protein may affect the spatial structure of both the peptide and the carrier protein. These results are likely to be of relevance for conformational peptide mimics in diagnostic tests, vaccine and inhibitors.