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VIRIP
Cat. No. AV-020
Structure:
Other Names:
Activity:
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.
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
Related areas
Technical Data
| Structure | H-Leu-Glu-Ala-Ile-Pro-Met-Ser-Ile-Pro-Pro-Glu-Val-Lys-Phe-Asn-Lys-Pro-Phe-Val-Phe-OH |
| Molecular Weight | 2302.24 |
| Formula | C112H171N23O27S |
| Sequence | LEAIPMSIPPEVKFNKPFVF |
| Modifications | None |
Solubility and Storage
| Solubility | Soluble in water |
| Appearance | Freeze dried solid |
| Storage | Store dry, frozen and in the dark |
Batch Specific Data
| Purity | >95% by hplc |
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Recent citations
A new publication from the University of Ljubljana uses MCA-AVLQSGFR-Lys(Dnp)-Lys-NH2, the FRET substrate for the severe acute respiratory syndrome coronavirus main protease (SARS-CoV Mpro), to determine the inhibitory potential of plant polyphenols
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