Nap-GFFKEH, Nap-1 peptide

Nap-GFFKEH, Nap-1 peptide

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

Nap-GFFKEH

naphthylacetic acid-Gly-Phe-Phe-Lys-Glu-His

6

95.1%

C₄₉H₅₇N₉O₁₀

932.03

Synthetic

Powder

Nap-1 is a noval class of histidine-containing hexapeptide derivatives used for in situ hydrogelation at the zinc ion-rich prostate tissue. Nap-1 displayed excellent self-assembly capability with a high sensitivity to zinc ions at about 0.1 equivalency. The molecular was rationally designed: (1) a dipeptide of phenylalanine (FF) which was utilized to promote molecular self-assembly and gelation; (2) a capping group of naphthalene to tune the hydrophobicity of Nap-1; (3) a terminus with glutamate (E) and histidine (H) to tune the hydrophilicity and to chelate zinc ions to form coordination bonds. Nap-1 was soluble in PBS and would form hydrogels at physiological pH (~pH 7.2) in the presence of zinc ions. The addition of 0.34 equiv. of EDTA destroyed the as-formed hydrogels of Nap-1 in 30 seconds, proving that metal chelations between zinc ions and peptides were vital for the self-assembly process.

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

• He S, Mei L, Wu C, et al. In situ hydrogelation of bicalutamide-peptide conjugates at prostate tissue for smart drug release based on pH and enzymatic activity. Nanoscale. 2019

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.