AS10 peptide

AS10 peptide

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

H-KLKKIAQKIKNFFQKLVP-OH

H-Lys-Leu-Lys-Lys-Ile-Ala-Gln-Lys-Ile-Lys-Asn-Phe-Phe-Gln-Lys-Leu-Val-Pro-OH

18

95.47%

C₁₀₅H₁₇₉N₂₇O₂₂

2171.7

Synthetic

Powder

Shorter peptides based on CRAMP, such as AS10 (KLKKIAQKIKNFFQKLVP), were also able to inhibit Candida albicans biofilm growth on Ti disks as well as formation of biofilms from other bacteria. The study also tested the effect of AS10 on human osteoblasts, mesenchymal stromal cells, and endothelial cells in vitro and demonstrated no negative effects on cell viability. Further, AS10 did not interfere with calcium deposition by the osteoblasts or mesenchymal stromal cells or with tube formation by the endothelial cells, which suggests that AS10 could be used as an anti-biofilm coating on implants without affecting cells in the surrounding tissues.

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

• De Brucker K et al (2014) Derivatives of the mouse cathelicidin-related antimicrobial peptide (CRAMP) inhibit fungal and bacterial biofilm formation. Antimicrob Agents Chemother 58:5395. https://doi.org/10.1128/AAC.03045-14

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.