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Products
Pharmacology
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- Technical support
- Resources
LIH383
Cat. No. PN-220
Structure:
H-Phe-Gly-Gly-Phe-Met-Arg-Arg-Lys-NH2
Activity:
Atypical chemokine receptor (ACKR3) agonist
LIH383 is a highly selective agonist of the atypical chemokine receptor, ACKR3 (formerly known as CXCR7). Functionally, ACKR3 is a scavenger receptor for a wide variety of opioid peptides, especially enkephalins and dynorphins, reducing their availability for the classical opioid receptors. LIH383 competes directly with CXCL12-AF647 for ACKR3 binding at low nanomolar concentrations and is more potent in inducing β-arrestin recruitment to ACKR3 than the full-length chemokine ligands CXCL12 and CXCL11, with EC50 values of 1.2 nM and 2.2 nM respectively, and no effect on of any other opioid or chemokine receptor at concentrations up to 3 µM. LIH383 can restrain the negative regulatory function of ACKR3 on opioid peptides and potentiate their activity in rat brain.
Meyrath et al (2020) The atypical chemokine receptor ACKR3/CXCR7 is a broad-spectrum scavenger for opioid peptides. Nat. Commun. 11 3033 PMID: 32561830
Szpakowska et al (2021) The natural analgesic conolidine targets the newly identified opioid scavenger ACKR3/CXCR7. Signal Transduct Target Ther. 6(1) 209 PMID: 34075018
Related areas
All peptides >
All chemokine receptor modulators >
All pain research categories >
Technical Data
| Structure | H-Phe-Gly-Gly-Phe-Met-Arg-Arg-Lys-NH2 |
| Molecular Weight | 997.23 |
| Formula | C45H72N16O8S |
| Sequence | FGGFMRRK-NH2 |
| Modifications | Amide at C terminal lysine |
Solubility and Storage
| Solubility | Soluble in water |
| Appearance | Freeze dried solid |
| Storage | Store desiccated, frozen and in the dark |
Batch Specific Data
| Purity | >95% by HPLC |
| Certificate of Analysis | PN-220 LIH383 0638-A0819 Product Datasheet_611e5dab17d77.doc |
| Safety Data Sheet | LIH383 MSDS_602be5b9154f4.pdf |
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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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