Pleurain-R1 peptide

Pleurain-R1 peptide

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

H-CVHWMTNTARTACIAP-OH

H-Cys-Val-His-Trp-Met-Thr-Asn-Thr-Ala-Arg-Thr-Ala-Cys-Ile-Ala-Pro-OH

16

95.94%

C₇₅H₁₁₉N₂₃O₂₁S₃

1775.08

Synthetic

Powder

Pleurain-R1 is an antioxidant and antimicrobial peptide identified from the skin secretions of Rana pleuraden (China, Asia), showing potent antioxidant and antibacterial activity.
Pleurain-R1 contains amino acid residues such as methionine, free cysteine, tyrosine, and proline, contributing to its antioxidant function.
The thiol group in Cys 10 of Pleurain-R1 is responsible for binding ABTS and reducing ABTS radical, indicating its antioxidant mechanism.
Pleurain-R1 is part of a diverse group of antioxidant peptides found in amphibian skin, highlighting the importance of proline residues in their antioxidant capabilities.
Pleurain-R1 also has Antibacterial, Antifungal activity. Active against E. coli (MIC 100 uM), S. aureus (MIC 25 uM), B. subtilis (MIC 100 uM), and C. albicans (MIC 50 uM).

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

• Yang H, Wang X, Liu X, et al. Antioxidant peptidomics reveals novel skin antioxidant system. Mol Cell Proteomics. 2009;8(3):571-83.
• Yan H, Liu Y, Tang J, Mo G, Song Y, Yan X, Wei L, Lai R. A novel antimicrobial peptide from skin secretions of the tree frog Theloderma kwangsiensis. Zoolog Sci. 2013 Sep;30(9):704-9.

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.