VIRIP peptide

VIRIP peptide

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

H-LEAIPMSIPPEVKFNKPFVF-OH

H-Leu-Glu-Ala-Ile-Pro-Met-Ser-Ile-Pro-Pro-Glu-Val-Lys-Phe-Asn-Lys-Pro-Phe-Val-Phe-OH

20

95.8%

C₁₁₂H₁₇₁N₂₃O₂₇S

2303.75

Synthetic

Powder

VIRIP is a natural subfragment of α1-antitrypsin (α1-AT) and is a broad-based inhibitor of HIV-1. VIRIP was identified from screening a human haemofiltrate derived library and corresponds to residues 353–37 of α1-AT, which is the most abundant circulating serine protease inhibitor. VIRIP directly targets the highly conserved viral gp41 fusion peptide to inhibit HIV-1 entry and inhibits a wide variety of HIV-1 strains including variants resistant to protease and reverse transcriptase inhibitors. VIRIP has little or no effect on infection by virions containing HIV-2, SIV, MLV, or VSV env proteins, or by other pathogens such as ebola, herpes simplex or respiratory syncytial virus.

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

• Münch et al (2007)Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. Cell 129(2) 263 PMID: 17448989
• Müller et al (2018) Reduced Susceptibility to VIRIP-Based HIV-1 Entry Inhibitors Has a High Genetic Barrier and Severe Fitness Costs. J Virol. 92(17) e00733-18 PMID: 29925662

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.