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[Gly14]-Humanin
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)]. 
This peptide 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, Aβ1-43-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.
| Code | Compound | Package |
| 4385-v | [Gly14]-Humanin | 0.5 mg vial |
| 4384-v | Humanin | 0.5 mg vial |
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