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Products
Pharmacology
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- Technical support
- Resources
VGN50
Cat. No. PP-320
Structure:
H-(D)Arg-Lys-Lys-Arg-Arg-Orn-Arg-Arg-Arg-βAla-Leu-Ser-Ser-Ile-Leu-Gln-Gly-Leu-Tyr-Gln-Leu-Asp-Thr-OH
Other Names:
K-Rta Peptide 1, Virus de Gann wo Naosu ORF50, K-Rta peptide
Activity:
Blocks MYC activation
VGN50 is a peptide derived from the Kaposi's sarcoma-associated herpes virus transactivator (K-Rta) sequence, based on the binding interface of K-Rta and cellular coactivators. VGN50 interacts with components of coactivators including nuclear receptor coactivator 2 (NCOA2), p300, and SWItch/Sucrose Non-Fermentable (SWI/SNF), the subfamily of ATP-dependent chromatin remodeling complex proteins. VGN50 blocks recruitment of the SWI/SNF complex and results in downregulation of both MYC and MYC-target gene transcription. Expression of MYC is tightly regulated in normal cells but becomes dysregulated in many types of human cancer cells, and application of VGN50 can reduce cell proliferation and selectively kill cancer cell lines in both tissue culture and a xenograft tumour mouse model.
Shimoda et al (2021) KSHV transactivator-derived small peptide traps coactivators to attenuate MYC and inhibits leukemia and lymphoma cell growth. Commun Biol. 4(1) 1330 PMID: 34857874
Related areas
All peptides >
All protein-protein interaction modulators >
All nuclear receptor modulators >
All cancer research categories >
Technical Data
| Structure | H-(D)Arg-Lys-Lys-Arg-Arg-Orn-Arg-Arg-Arg-βAla-Leu-Ser-Ser-Ile-Leu-Gln-Gly-Leu-Tyr-Gln-Leu-Asp-Thr-OH |
| Molecular Weight | 2827.70 |
| Formula | C121H218N46O32 |
| Sequence | rKKRR-Orn-RRR-βAla-LSSILQGLYQLDT |
| Modifications | D arginine at position 1, ornithine at position 6 and beta alanine at position 10 |
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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