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Products
Pharmacology
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- Technical support
- Resources
PD-L1Pep-2
Cat. No. PP-380
Structure:
H-Cys-Val-Arg-Ala-Arg-Thr-Arg-OH
Other Names:
PD-L1-blocking peptide
Activity:
Binds to PD-L1
PD-L1Pep-2 was identified from a phage-displayed library for peptides that selectively bind to PD-L1-overexpressing cells. PD-L1Pep-2 has a binding affinity of 281 nM, and preferentially binds to high PD-L1-expressing cells over low PD-L1-expressing cells, binding further enhanced by interferon-γ, an inducer of PD-L1 expression. In animal models, intravenously injected PD-L1Pep-2 efficiently targets tumour tissues, inhibits tumour growth, and increases the CD8+/FoxP3+ ratio in mice. PD-L1Pep-2 in combination with doxorubicin inhibits tumour growth more efficiently than doxorubicin alone. PD-L1Pep-2 blockade of PD-L1 reinvigorates T-cell activity and inhibits tumour growth by enhancing anti-tumour immunity.
Gurung et al (2020) Phage display-identified PD-L1-binding peptides reinvigorate T-cell activity and inhibit tumor progression. 247 119984 PMID: 32278214
Park et al (2022) Abstract 3422: Combined treatment with interleukin-4 receptor-targeted cytotoxic peptide and PD-L1-blocking peptide efficiently induces immunogenic cell death of tumor cells and activates T-cell activity. Cancer Res 82 (12 Supplement) 3422. https://doi.org/10.1158/1538-7445.AM2022-3422
Related areas
All peptides >
All protein-protein interaction modulators >
All cancer research categories >
Technical Data
| Structure | H-Cys-Val-Arg-Ala-Arg-Thr-Arg-OH |
| Molecular Weight | 860.48 |
| Formula | C33H64N16O9S |
| Sequence | CVRARTR |
| 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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