Combi-1 peptide

Combi-1 peptide

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

RRWWRF

Arg-Arg-Trp-Trp-Arg-Phe

6

98.2%

Synthetic

Powder

N-terminal acetylation and C-terminal amidation. Also active against E. coli ATCC 2592, M. luteus, and S. cerevisae Ke T et al., 2012. 3D structure in SDS or DPC micelles was reported by Jing W, Hunter HN, Hagel J, Vogel HJ in J Pept Res. 2005 May;65(5):491-501 and the authors propose that the main bactericidal site of action of these peptides might be located inside bacteria. Cyclization improves both antimicrobial activity and cell selectivity (Dathe et al 2004 Biochemistry 43: 9140-50). Combi-1 has Antimicrobial activity. Combi-1 was found in Synthetic Combinatorial peptide Library.

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

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.