AGA-(C8R) HNG17, humanin derivative peptide

• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

AGA-(C8R)HNG17 is a potent derivative of the Humanin (HN) peptide, characterized by specific amino acid modifications that enhance its neuroprotective properties. This 17-residue peptide incorporates an Ala-Gly-Ala (AGA) N-terminal sequence and an Arg substitution at position 8 (C8R), which collectively improve its stability and bioactivity. The peptide exhibits robust neuroprotective effects against amyloid-β (Aβ)-induced toxicity and other Alzheimer’s disease-relevant insults at picomolar concentrations in vitro.

The structural modifications in AGA-(C8R)HNG17, including the C8R substitution and truncation to the core 17-amino acid sequence (HNG17), contribute to its heightened efficacy compared to the native HN peptide. These alterations optimize its interaction with cellular targets, such as the STAT3 signaling pathway, while maintaining its resistance to proteolytic degradation. The peptide’s mechanism involves suppression of neuronal apoptosis triggered by Aβ and familial Alzheimer’s disease-linked mutations, highlighting its potential as a research tool for studying neuroprotection.

• Chiba T, Yamada M, Hashimoto Y, Sato M, Sasabe J, Kita Y, Terashita K, Aiso S, Nishimoto I, Matsuoka M. Development of a femtomolar-acting humanin derivative named colivelin by attaching activity-dependent neurotrophic factor to its N terminus: characterization of colivelin-mediated neuroprotection against Alzheimer's disease-relevant insults in vitro and in vivo. J Neurosci. 2005 Nov 2;25(44):10252-61. doi: 10.1523/JNEUROSCI.3348-05.2005. PMID: 16267233; PMCID: PMC6725789.

Trifluoroacetic acid (TFA) is a common counterion from the purification process using High-Performance Liquid Chromatography (HPLC). The presence of TFA can affect the peptide's net weight, appearance, and solubility.

Impact on Net Weight: The TFA salt contributes to the total mass of the product. In most cases, the peptide content constitutes >80% of the total weight, with TFA accounting for the remainder.

Solubility: TFA salts generally enhance the solubility of peptides in aqueous solutions.

In Biological Assays: For most standard in vitro assays, the residual TFA levels do not cause interference. However, for highly sensitive cellular or biochemical studies, please be aware of its presence.