NH2-UAMC1110 is a peptide-inspired scaffold with defined aromatic and polar features that support targeted binding. Researchers explore its structure using spectroscopic tools to characterize conformational equilibria. Applications include ligand screening, PPI modeling, and SAR evaluation.
CAT No: R2819
Synonyms/Alias:NH2-UAMC1110; 2758337-19-6; UAMC1110-NH2; SCHEMBL23531732; UAMC1110-NH2?; EX-A7847R; HY-153552; CS-0783398; (S)-6-(4-Aminobutoxy)-N-(2-(2-cyano-4,4-difluoropyrrolidin-1-yl)-2-oxoethyl)quinoline-4-carboxamide; 6-(4-aminobutoxy)-N-[2-[(2S)-2-cyano-4,4-difluoropyrrolidin-1-yl]-2-oxoethyl]quinoline-4-carboxamide
NH2-UAMC1110 is a synthetic peptide compound designed for advanced biochemical research applications. Characterized by its N-terminal amino group and unique sequence architecture, this peptide is engineered to facilitate studies in protease activity, substrate specificity, and enzyme kinetics. Its tailored structure enables precise interrogation of proteolytic mechanisms and supports the development of novel biochemical assays. As a research-use tool, NH2-UAMC1110 offers significant value for scientists investigating enzyme function, substrate profiling, and peptide-based assay development.
Enzyme Substrate Profiling: In protease research, NH2-UAMC1110 serves as a valuable substrate for characterizing enzyme specificity and catalytic efficiency. Its defined peptide sequence allows researchers to examine the cleavage preferences of various proteases, supporting the identification of substrate recognition motifs and the elucidation of enzymatic mechanisms. By enabling accurate mapping of protease-substrate interactions, the compound contributes to a deeper understanding of proteolytic regulation in physiological and pathological contexts.
Assay Development: The compound is frequently utilized in the design and optimization of in vitro biochemical assays targeting protease activity. Its stability and well-defined structure make it an ideal candidate for use in fluorogenic, colorimetric, or mass spectrometry-based assay platforms. Integration of NH2-UAMC1110 into assay systems enhances sensitivity and reproducibility, facilitating high-throughput screening of enzyme inhibitors, activators, or modulators within drug discovery and basic research pipelines.
Peptide-Protein Interaction Studies: NH2-UAMC1110 is suitable for probing peptide-protein interactions, particularly in the context of enzyme-substrate or receptor-ligand binding investigations. By incorporating this synthetic peptide into binding assays, researchers can dissect the molecular determinants of specificity, affinity, and allosteric regulation. Such studies provide critical insights into protein function, signaling cascades, and the structural basis of molecular recognition events.
Structure-Activity Relationship Analysis: The compound is instrumental in structure-activity relationship (SAR) studies aimed at optimizing peptide substrates or inhibitors for target enzymes. Modifications to its sequence or terminal groups can be systematically evaluated to determine the impact on enzymatic processing or binding affinity. This approach enables rational design of improved peptide probes and supports the development of selective biochemical tools for mechanistic studies.
Analytical Method Validation: NH2-UAMC1110 is also employed as a reference standard or calibration substrate in analytical method development for protease quantification and activity assessment. Its consistent performance and defined molecular properties make it suitable for validating assay linearity, sensitivity, and specificity. Use of this peptide in analytical workflows ensures robust data quality and supports the reliable measurement of enzymatic activity in complex biological samples.
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