LIH383 is a peptide-based inhibitor scaffold characterized by aromatic and hydrophobic residues that target structured protein interfaces. Its backbone supports extended or helical conformations depending on solvent. Researchers assess its stability, binding kinetics, and interaction hotspots. Applications include PPI modulation, inhibitor design, and mechanistic structural biology.
CAT No: R2802
Synonyms/Alias:LIH383; CHEMBL5194677; BDBM50589879; HY-P10333; CS-1051166
LIH383 is a small-molecule biochemical compound recognized for its potent and selective inhibition of casein kinase 1 delta (CK1δ). As a non-peptide kinase inhibitor, LIH383 has become a valuable research tool for dissecting the regulatory mechanisms of CK1δ within cellular signaling networks. Its high specificity and well-characterized mode of action make it particularly relevant for studies exploring the roles of CK1 isoforms in circadian rhythm regulation, signal transduction, and neurobiology. By enabling targeted modulation of CK1δ activity, LIH383 supports advanced investigations into phosphorylation-dependent processes critical for cellular homeostasis and disease modeling.
Kinase inhibition studies: LIH383 serves as a reliable chemical probe for the selective inhibition of CK1δ kinase activity in vitro and in cell-based assays. Researchers leverage its structural and functional properties to delineate the contributions of CK1δ-mediated phosphorylation events in various biological pathways. The compound's specificity facilitates the dissection of CK1δ's role without significant off-target effects on related kinases, thereby enabling precise mechanistic studies and functional mapping of phosphorylation cascades.
Circadian biology research: The compound is widely used to investigate the molecular underpinnings of circadian rhythms, given CK1δ's established involvement in the regulation of core clock proteins such as PER and CRY. By modulating CK1δ activity with LIH383, scientists can assess the impact on period length, phase shifts, and the stability of circadian oscillators in cellular and ex vivo systems. This application provides valuable insights into the temporal regulation of gene expression and the molecular architecture of the circadian clock.
Signal transduction pathway analysis: LIH383 is employed to interrogate the role of CK1δ in diverse signaling pathways, including Wnt/β-catenin, DNA damage response, and cell cycle control. Its use allows for the targeted disruption of CK1δ-dependent phosphorylation, facilitating the study of downstream signaling events and the identification of CK1δ substrates. Such analyses are instrumental in elucidating the broader functional landscape of casein kinase 1 family members in cellular physiology.
Neurobiological mechanism exploration: The compound is instrumental in research focused on the neurobiology of learning, memory, and neurodegenerative disease models. CK1δ has been implicated in the phosphorylation of proteins involved in synaptic plasticity and neuronal signaling. With LIH383, investigators can selectively inhibit CK1δ to probe its influence on neuronal function, synaptic remodeling, and protein aggregation processes in vitro and in relevant animal models.
Drug discovery and target validation: LIH383 is also utilized in early-stage drug discovery efforts as a reference inhibitor for CK1δ. Its well-characterized inhibitory profile makes it an ideal comparator in high-throughput screening, structure-activity relationship (SAR) studies, and target validation experiments. By benchmarking the activity of novel CK1δ modulators against LIH383, researchers can more effectively assess compound selectivity, potency, and potential off-target liabilities during the lead optimization process.
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