Abstract: The crystal structure of a new designed hapten N-benzoyl tauryl phenylalanine was studied by XRD . The results showed that the configuration of sulfur atom is tetrahedron,-SO₂NH-is close to transition state of amide hydrolysis and there are severa LIN termolecular hydrogen bonds. The crystal structure was optimized by Molgen program, and then compared with the hapten that contain phosphorus. The conformation analysis of N-S-C and N-P-C bonds showed that N-S-C had only one single low energy conformer. Their charges were also calculated by MOPAC program(AM1 calculation), and it is found that the charge distribution around Satom is very close to that of the Patom. Those results showed that the molecule could be used to induce antibodies with CPA activity.

Key words: Antibody enzyme, Hapten enzyme, Molecular design, Peptide hydrolysis