Novel Biological Activity of the Region (106—126) on Human Prion Sequence

Abstract

We report that the synthetic peptide Prp106—126 (KTNMKHMAGAAAAGAVVGGLG-COOH) and the reversed peptide Prp126—106 (GLGGVVAGAAAAGAMHKMNTK-COOH) of human prion (hPrp) can express the decarboxylase activity for oxaloacetate in the presence of trifluoroethanol, similar to that of Oxaldie 1 (LAKLLKALAKLLKK-CONH₂) reported previously. The degree of the relative activity of Prp106—126 and Prp126—106 to Oxaldie 1 is 0.47 and 0.21, respectively. Based on this experimental result, we applied the informational system method (ISM) developed by Veljkovic et al. to the amino acid sequence of Prp106—126 and Prp126—106 to extract a common factor. The same spectra were obtained, indicating that the same periodicity may be conserved on their sequences, as a necessary factor for expressing the same biological activity, irrespective of the orientation of the primary sequence.