Urumin peptide

Urumin peptide

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

H-IPLRGAFINGRWDSQCHRFSNGAIACA-OH

H-Ile-Pro-Leu-Arg-Gly-Ala-Phe-Ile-Asn-Gly-Arg-Trp-Asp-Ser-Gln-Cys-His-Arg-Phe-Ser-Asn-Gly-Ala-Ile-Ala-Cys-Ala-OH

27

95.67%

C₁₂₉H₁₉₈N₄₂O₃₅S₂

2961.33

Synthetic

Powder

Urumin is a 27-amino acid virucidal host defense peptide, originally isolated from the skin of the South Indian frog Hydrophylax bahuvistara. Urumin is virucidal for H1 hemagglutinin bearing human influenza A viruses, in which it specifically targets the conserved stalk region of H1 hemagglutinin, and is effective against drug-resistant H1 influenza viruses that are resistant to oseltamivir, zanamivir and peramivir. Urumin appears to inhibit viral growth by physically destroying influenza virions, and can also protect naive mice from lethal influenza infection in vivo.

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

• Holthausen et al (2017) An Amphibian Host Defense Peptide Is Virucidal for Human H1 Hemagglutinin-Bearing Influenza Viruses. Immunity 46(4) 587 PMID: 28423338

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.