The abnormal accumulation of the peptide amyloid-beta in the form of senile (or amyloid) plaques is one of the hallmarks of Alzheimer's disease (AD). Zinc ions have been implicated in AD and plaques formation. Recently, the peptide humanin has been discovered. Humanin showed neuroprotective activity against amyloid-beta insults. Here the question investigated is if humanin could interact directly with Zn(II). It is shown that Zn(II) and its substitutes Cd(II)/Co(II) bind to humanin via a thiolate bond from the side chain of the single cysteine at position 8. The low intensity of the d-d bands of Co(II)-humanin indicated an octahedral coordination geometry. Titration experiments suggest that Zn(II) binds to humanin with an apparent affinity in the low muM range. This apparent Zn-binding affinity is in the same order as for amyloid-beta and glutathione and could thus be of physiological relevance.
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[Gly14]-Humanin ameliorates high glucose-induced endothelial senescence via SIRT6.
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Article Synopsis
- Preserving hair cells is essential for hearing, as their damage is linked to permanent hearing loss and is often caused by inflammation and oxidative stress.
- Mitochondrial-derived peptides (MDPs), especially Humanin (HN) and its synthetic variant HN S14G (HNG), have shown protective effects on hair cells, with HNG being more potent than natural HN.
- Research revealed that HNG and the lesser-known peptide SHLP3 can reduce hair cell loss caused by gentamicin, primarily by regulating key proteins and decreasing oxidative stress and inflammation, suggesting potential therapeutic uses for these peptides in combating hearing loss.
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