An elective, selective inhibitor of the mast cell tryptase, which inhibits tryptase-induced histamine release from human tonsil and lung cells. It can reduce airway inflammation and block postchallenge airway hyperresponsiveness in vivo.
CAT No: R0892
CAS No:158921-85-8
Synonyms/Alias:N-(1-Hydroxy-2-naphthoyl)-L-arginyl-L-prolinamide
APC 366 is a synthetic peptide compound recognized for its role as a potent and selective inhibitor of human dipeptidyl peptidase IV (DPP-IV), an enzyme involved in the regulation of bioactive peptides. As a structurally defined peptide, APC 366 offers valuable utility in biochemical research focused on protease activity, signal transduction, and the modulation of peptide-mediated pathways. Its high specificity for DPP-IV makes it an essential molecular tool for dissecting the physiological and pathological functions of this enzyme in various experimental systems. Researchers leverage APC 366 to elucidate the intricate relationships between peptide processing, metabolic regulation, and cellular communication.
Enzyme inhibition studies: APC 366 is widely utilized in enzymology to investigate the mechanistic aspects of DPP-IV activity. By serving as a selective inhibitor, it allows researchers to precisely modulate DPP-IV function in vitro, facilitating the assessment of substrate specificity, catalytic kinetics, and inhibitor binding dynamics. The ability to control DPP-IV activity using APC 366 enables detailed exploration of protease-substrate interactions and aids in the validation of novel assay platforms for high-throughput screening of related enzyme inhibitors.
Peptide signaling research: In studies of peptide hormone regulation and signal transduction, APC 366 provides a means to block DPP-IV-mediated degradation of endogenous peptides such as incretins, neuropeptides, and chemokines. This functional blockade is instrumental in mapping the downstream effects of stabilized bioactive peptides on cellular pathways, receptor activation, and gene expression profiles. By preserving peptide integrity, APC 366 helps clarify the physiological roles of DPP-IV substrates and the broader impact of proteolytic processing in cell signaling networks.
Metabolic pathway analysis: The inhibition of DPP-IV by APC 366 is particularly relevant to metabolic research, where it is employed to study the enzyme's influence on glucose homeostasis, lipid metabolism, and energy balance. Through selective suppression of DPP-IV activity, investigators can dissect the contributions of peptide hormones and their metabolites to metabolic pathways in cell-based models, tissue preparations, or ex vivo systems. This approach supports the identification of novel metabolic regulators and enhances understanding of the interplay between protease activity and metabolic control.
Protease selectivity profiling: APC 366 serves as a reference inhibitor in the characterization of DPP-IV selectivity relative to other serine proteases. Its well-defined inhibitory profile allows for comparative studies assessing cross-reactivity, off-target effects, and the structural determinants of enzyme specificity. Such profiling is essential for the rational design of next-generation protease inhibitors and for distinguishing DPP-IV-dependent phenomena from those involving related enzymes in complex biological samples.
Peptide-based drug discovery research: The application of APC 366 extends to early-stage drug discovery, where it is used to validate DPP-IV as a target for peptide-based therapeutic development. By providing a reliable tool for functional inhibition, APC 366 enables the screening of compound libraries, the evaluation of structure-activity relationships, and the optimization of lead candidates targeting protease-mediated pathways. Its use in these contexts accelerates the translation of fundamental enzymology into practical strategies for the modulation of peptide-processing enzymes in research settings.
In sheep naturally sensitized to Ascaris suum , the novel selective inhibitor of tryptase APC 366 [N-(1-hydroxy-2-naphthoyl)-L-arginyl-L-prolinamide] attenuates the EAR, the LAR, acquired BHR, and the accompanying influx of inflammatory leukocytes on aerosol challenge with an antigenic extract. It has been shown that APC 366 inactivates tryptase in a time-dependent and irreversible manner involving slow isomerization of the hydroxynaphthyl group of APC 366 followed by nucleophilic attack of a tryptase amino acid side chain to result in the formation of a nonhydrolyzable covalent adduct between inhibitor and enzyme.
Inhibition of mast cell tryptase by inhaled APC 366 attenuates allergen-induced late-phase airway obstruction in asthma
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