ChemicalBook--->CAS DataBase List--->676657-00-4

676657-00-4

676657-00-4 Structure

676657-00-4 Structure
IdentificationBack Directory
[Name]

KYL
[CAS]

676657-00-4
[Synonyms]

KYL
KYL peptide
L-Leucine, L-lysyl-L-tyrosyl-L-leucyl-L-prolyl-L-tyrosyl-L-tryptophyl-L-prolyl-L-valyl-L-leucyl-L-seryl-L-seryl-
[Molecular Formula]

C74H108N14O17
[MDL Number]

MFCD30182273
[MOL File]

676657-00-4.mol
[Molecular Weight]

1465.73
Chemical PropertiesBack Directory
[Boiling point ]

1728.5±65.0 °C(Predicted)
[density ]

1.290±0.06 g/cm3(Predicted)
[storage temp. ]

Store at -20°C
[solubility ]

Soluble in DMSO
[form ]

Solid
[pka]

3.29±0.10(Predicted)
[color ]

White to off-white
[Water Solubility ]

Soluble to 2 mg/ml in water
[Sequence]

H-Lys-Tyr-Leu-Pro-Tyr-Trp-Pro-Val-Leu-Ser-Ser-Leu-OH
[InChIKey]

FZNPYIAZMDBRLC-RKNDTPCJSA-N
Safety DataBack Directory
[WGK Germany ]

WGK 3
[Storage Class]

11 - Combustible Solids
Hazard InformationBack Directory
[Uses]

KYL peptide, an antagonistic peptide, selectively targets EphA4 receptor (IC50:4.22 μM, Kd:1.3 μM). KYL peptide binds to the ligand-binding domain of EphA4, effectively alleviates Aβ-induced synaptic dysfunction and synaptic plasticity defects in AD mice. KYL peptide can promote nerve regeneration after injury and modulating immune responses[1][2][3].
[Biological Activity]

KYL is a potent and selective EphA4 receptor tyrosine kinase antagonist th at inhibits EphA4-EphrinA5 interactions. KYL binds to the ephrin-binding domain of EphA4.
[IC 50]

EphA4: 4.22 μM μM (IC50); EphA4: 1.30 μM (Ki)
[storage]

Store at -20°C
[References]

[1] Wu B, et.al. HTS by NMR of combinatorial libraries: a fragment-based approach to ligand discovery. Chem Biol. 2013 Jan 24;20(1):19-33. DOI:10.1016/j.chembiol.2012.10.015
[2] Lamberto I, et, al. Distinctive binding of three antagonistic peptides to the ephrin-binding pocket of the EphA4 receptor. Biochem J. 2012 Jul 1;445(1):47-56. DOI:10.1042/BJ20120408
[3] Fu AKY, et, al. Blockade of EphA4 signaling ameliorates hippocampal synaptic dysfunctions in mouse models of Alzheimer's disease. Proc Natl Acad Sci U S A. 2014 Jul 8;111(27):9959-64. DOI:10.1073/pnas.1405803111
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