GHK Peptide Prevents Metal-Induced Protein Aggregation and Brain Cell Death In Vitro

Many neurodegenerative diseases, such as Alzheimer's and Parkinson's, are characterized by oxidative stress, inflammation, and the harmful misfolding of proteins. An excess of free metal ions, particularly copper and zinc, is known to strongly promote this damaging protein aggregation and contribute to central nervous system (CNS) cell death. This study specifically investigates whether the endogenous tripeptide glycyl-l-histidyl-l-lysine (GHK) can counteract copper and zinc toxicity and prevent protein aggregation in laboratory settings.

The study demonstrated that GHK effectively binds to copper ions and reduces their redox activity, thereby mitigating a key source of oxidative stress. GHK was found to significantly prevent both copper- and zinc-induced cell death in central nervous system cell models, offering crucial cytoprotection. Moreover, GHK not only prevented the aggregation of bovine serum albumin induced by copper and zinc but also remarkably reversed existing protein aggregation, effectively resolubilizing the proteins. In inflammatory conditions, where copper toxicity was enhanced, GHK was shown to attenuate this increased toxicity, and it also provided a protective effect against paraquat toxicity when exacerbated by copper.