ZP 120C is a potent and selective inhibitor that targets the protein kinase Aurora A. This innovative compound has shown promising results in preclinical studies for the treatment of various cancers, particularly in inhibiting tumor cell proliferation. Its use is being explored in combination with existing chemotherapy drugs to enhance their efficacy and overcome drug resistance mechanisms.
CAT No: R1996
CAS No:383123-18-0
Chemical Name:(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-acetamido-5-(diaminomethylideneamino)pentanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-6-aminohexanoyl]amino]-6-aminohexanoyl]amino]-6-aminohexanoyl]amino]-6-aminohexanoyl]amino]-6-aminohexanoyl]amino]-6-aminohexanoyl]amino]-6-aminohexanamide
ZP 120C is a synthetic peptide compound designed for advanced biochemical and physiological research applications. As a member of the peptide class, it comprises a specific sequence of amino acids tailored to interact selectively with biological targets, making it a valuable tool for probing molecular mechanisms in cellular systems. Its unique structure and functional properties enable researchers to investigate signal transduction pathways, receptor-ligand interactions, and protein-protein communication with high specificity. ZP 120C is recognized for its ability to modulate and mimic endogenous peptide functions, thus facilitating the study of complex biochemical networks in a controlled experimental context.
Peptide receptor research: ZP 120C is frequently employed to study peptide-mediated signaling pathways, particularly those involving G-protein-coupled receptors (GPCRs) and other membrane-bound peptide receptors. By serving as a selective ligand or modulator, it allows researchers to dissect receptor activation, downstream effector engagement, and feedback mechanisms within cellular models. This contributes to a deeper understanding of receptor specificity, affinity, and the broader physiological roles of peptide signaling.
Functional assay development: The compound is instrumental in the creation and optimization of in vitro and cell-based assays designed to quantify biological responses to peptide stimulation. Its defined sequence and activity profile make it an ideal standard or control in high-throughput screening platforms, facilitating the assessment of receptor activation, second messenger generation, or other functional endpoints. Utilizing ZP 120C in these assays supports the validation of novel drug candidates and the elucidation of cellular response dynamics.
Structure-activity relationship (SAR) studies: ZP 120C serves as a reference molecule for systematic modifications and analog synthesis aimed at mapping critical residues responsible for biological activity. By comparing its activity to that of structurally related peptides, researchers can identify key determinants of potency, selectivity, and stability. Such SAR investigations are pivotal for guiding the rational design of next-generation peptide analogs with improved pharmacological profiles for research purposes.
Protein-protein interaction analysis: The peptide's defined sequence and binding characteristics enable its use in studies of protein-protein interactions, particularly those mediated by short peptide motifs. Techniques such as surface plasmon resonance (SPR), isothermal titration calorimetry (ITC), and co-immunoprecipitation benefit from the use of ZP 120C as a probe to quantify binding affinities, kinetics, and specificity between interacting partners. Insights gained from these studies advance the understanding of cellular signaling complexes and regulatory networks.
Peptide stability and degradation research: ZP 120C is also utilized to investigate the enzymatic stability and metabolic fate of peptides in biological matrices. By monitoring its degradation profile in cell lysates, plasma, or tissue homogenates, researchers can assess the influence of proteases and other modifying enzymes on peptide half-life and bioavailability. These studies inform the development of more stable peptide analogs and provide foundational data on peptide turnover in experimental systems.
2. The spatiotemporal control of signalling and trafficking of the GLP-1R
4. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
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