[Gly¹⁴]-Humanin

Met – Ala – Pro – Arg – Gly – Phe – Ser – Cys – Leu – Leu – Leu – Leu – Thr – Gly – Glu – Ile – Asp – Leu – Pro – Val – Lys – Arg – Arg – Ala

Synthetic Product (Trifluoracetate Form)

The purity is guaranteed to be higher than 99% by HPLC
[Gly14]Humanin contains a single cysteine residue and shows a tendency to form dimers. Please use fresh preparations only and do not store aliquots in a freezer.

Potent Rescue Factor Abolishing Neuronal Cell Death

[Gly¹⁴]-Humanin a new tool for Alzheimer’s Disease Research

Through functional expression screening (termed a death-trap screening), Professor Nishimoto (KEIO University) and his colleagues identified a cDNA, encoding a novel 24-amino acid-residue peptide, designated as " humanin " [Proc. Natl. Acad. Sci. U.S.A., 98, 6336-6341 (2001)]. Humanin abolishes death of neuronal cells caused by multiple different types of familial Alzheimer’s disease gene products and Aβ amyloid. Transfection of a plasmid encoding humanin cDNA to F11 neuronal cells suppressed toxicity by either V642I-APP, M146L-PS1, or N141I-PS2 cDNA. The cultured medium of F11 cells transfected with plasmid humanin carried protective activity, and contained bands of the humanin immunoreactivity at 3-4 kDa. Humanin was thus transcribed from coding death-trap clones and secreted into the medium. Synthetic humanin protected V642I-APP-transfected F11 cells from death in a dose- dependent manner. After structure-activity relationship study, they found potent analog, that is, a Ser to Gly substituted peptide at position 14. This analog is 1000 times more potent than that of the parent peptide humanin. The [Gly¹⁴]-humanin (10 nM) blocks V642I-APP, M146L-PS1, and N141I-PS2 cDNA-induced cell-death. When neurons are pretreated with 10 nM of [Gly¹⁴]-humanin, Aβ 1-43-induced death as well as dystrophic changes of neurites are suppressed. Although further experiments are required, this potent [Gly¹⁴]-humanin will contribute to generate the new Alzheimer’s disease therapeutics targeting for neuroprotection.

References:

1. Y. Hashimoto, T. Niikura, H. Tajima, T. Yasukawa, H. Sudo, Y. Ito, Y. Kita, M. Kawasumi, K. Kouyama, M. Doyu, G. Sobue, T. Koide, S. Tsuji, J. Lang, K. Kurokawa and I. Nishimoto, Proc. Natl. Acad. Sci. USA, 98, 6336 (2001) (Original)
2. Y. Hashimoto, Y. Ito, T. Niikura, Z. Shao, M. Hata, F. Oyama and I. Nishimoto, Biochem. Biophys. Res. Commun., 283, 460 (2001) (Pharmacol.)