Novel biological activity of the region (106-126) on human prion sequence.
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.
Numao
Naganori
N
BioFrontier Institute Inc. Kanagawa, Japan. numao-n@sssc.co.jp
Noguchi
Norihisa
N
Eguchi
Yukihiro
Y
Watanabe
Satoshi
S
Fukui
Tetsuya
T
Kamino
Tomoyuki
T
Shimozono
Noriko
N
Yamazaki
Akiko
A
Kobayashi
Susumu
S
Sasatsu
Masanori
M
D000595:Amino Acid Sequence / Q000187:drug effects / Q000502:physiology; D002262:Carboxy-Lyases / Q000378:metabolism; D004789:Enzyme Activation / Q000187:drug effects / Q000502:physiology; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000235:genetics / Q000493:pharmacokinetics / Q000494:pharmacology*; D011328:Prions / Q000235:genetics* / Q000493:pharmacokinetics / Q000494:pharmacology*
D010446:Peptide Fragments; D011328:Prions; D002262:Carboxy-Lyases