2012 peptide

2012 peptide

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

Batch to batch variation of the purity

Myr-NLR8ELDRLLS5ELN-NH2

Myr-Asn-Leu-Arg-Glu-Leu-Asp-Arg-Leu-Leu-Ser-Glu-Leu-Asn-NH2

13

95.42%

C₈₁H₁₄₄N₂₂O₂₃

1794.13

Synthetic

Powder

R8：(R)-2-(7 - octenyl) alanine (unstapled)，S5：(S)-2-(4 - pentenyl) alanine.
Peptide 2012 is a myristoylated analog of peptide 1907. It's designed to target the FAK-paxillin interaction. It has enhanced cellular permeability, with significant uptake increases in melanoma cells. It shows high proteolytic resistance. Functionally, it disrupts FAK localization to focal adhesions, reducing the number of FAK-containing focal adhesions in a dose-dependent manner. It has selective anti-cancer effects, reducing cancer cell viability in melanoma and glioblastoma cell lines without affecting normal cells much. It also induces apoptosis and inhibits cancer cell invasion. In terms of pharmacokinetics, it has good plasma and metabolic stability, a long plasma half-life of 16.5 h in mice. In the B16F10 melanoma mouse model, it significantly reduces tumor burden and is well-tolerated.

Normally, this peptide will be delivered in lyophilized form and should be stored in a freezer at or below -20 °C. For more details, please refer to the manual: Handling and Storage of Synthetic Peptides

• Reyes L, Naser L, Weiner WS, Thifault D, Stahl E, McCreary L, Nott R, Quick C, Buchberger A, Alvarado C, Rivera A, Miller JA, Khatiwala R, Cherry BR, Nelson R, Martin-Garcia JM, Stephanopoulos N, Fromme R, Fromme P, Cance W, Marlowe T. Structure-based discovery of hydrocarbon-stapled paxillin peptides that block FAK scaffolding in cancer. Nat Commun. 2025 Feb 28;16(1):2060. doi: 10.1038/s41467-025-57196-9. PMID: 40021642; PMCID: PMC11871066.

Trifluoroacetic acid (TFA) has a significant impact on peptides due to its role in the peptide synthesis process.

TFA is essential for the protonation of peptides that lack basic amino acids such as Arginine (Arg), Histidine (His), and Lysine (Lys), or ones that have blocked N-termini. As a result, peptides often contain TFA salts in the final product.

TFA residues, when present in custom peptides, can cause unpredictable fluctuations in experimental data. At a nanomolar (nM) level, TFA can influence cell experiments, hindering cell growth at low concentrations (as low as 10 nM) and promoting it at higher doses (0.5–7.0 mM). It can also serve as an allosteric regulator on the GlyR of glycine receptors, thereby increasing receptor activity at lower glycine concentrations.

In an in vivo setting, TFA can trifluoroacetylate amino groups in proteins and phospholipids, inducing potentially unwanted antibody responses. Moreover, TFA can impact structure studies as it affects spectrum absorption.