antifouling zwitterionic peptide

antifouling zwitterionic peptide

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

H-CFEFKFC-OH

H-Cys-Phe-Glu-Phe-Lys-Phe-Cys-OH

7

95.95%

C₄₄H₅₈N₈O₁₀S₂

923.1

Synthetic

Powder

It has the properties of antifouling zwitterionic peptide hydrogel, and can be used in fabricating electrochemical biosensors.The zwitterionic peptide hydrogel with cysteine terminal is easy for immobilization onto the gold surface, and it is also suitable for the immobilization of biomolecules such as antibodies, through the formation of covalent amide bonds. The peptide hydrogel possessed excellent antifouling property, and it was able to effectively prevent the adsorption of nonspecific proteins, cells and other biomolecules.

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

• Du Q, Wang W, Zeng X, Luo X. Antifouling zwitterionic peptide hydrogel based electrochemical biosensor for reliable detection of prostate specific antigen in human serum. Anal Chim Acta. 2023 Jan 25;1239:340674. doi: 10.1016/j.aca.2022.340674. Epub 2022 Nov 24. PMID: 36628704.

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.