Boc-DL-Leu-DL-Ser-DL-xiThr-DL-Arg-AMC is a mixed-chirality peptide featuring an AMC fluorophore that enables sensitive detection of enzymatic turnover. The Boc-protected N-terminus stabilizes the substrate during synthetic manipulation. Researchers use it to examine protease specificity, catalytic behavior, and polarity-driven interactions. Its diverse residue set enhances conformational variability.
CAT No: R2260
CAS No:73554-93-5
Synonyms/Alias:Boc-leu-ser-thr-arg-mca;73554-93-5;Boc-Leu-Ser-Thr-Arg-AMC trifluoroacetate salt;Boc-Leu-Ser-Thr-Arg-7-amido-4-methylcoumarin;Boc-Leu-Ser-Thr-Arg-AMC;MLS-3112-V;Boc-Leu-Ser-Thr-Arg-7-amido-4-methylcoumarin, protein C substrate;t-Butyloxycarbonyl-L-Leucyl-L-Seryl-L-Threonyl-L-Arginine 4-Methyl-Coumaryl-7-Amide; Boc-Leu-Ser-Thr-Arg-MCA; Boc-LSTR-AMC;
Boc-DL-Leu-DL-Ser-DL-xiThr-DL-Arg-AMC is a synthetic peptide substrate featuring a protected N-terminus (Boc group), a defined sequence of mixed-configuration amino acid residues, and a C-terminal 7-amino-4-methylcoumarin (AMC) fluorogenic tag. This compound is designed for use in biochemical assays that require precise monitoring of proteolytic activity, particularly in systems where stereochemical diversity and sequence specificity are critical. The presence of both D- and L-amino acid residues within the peptide backbone offers unique resistance profiles and substrate selectivity, while the AMC moiety enables sensitive fluorescence-based detection. As such, this molecule serves as a valuable research tool for elucidating protease mechanisms, validating enzyme selectivity, and optimizing assay protocols in peptide biochemistry and enzymology.
Enzyme activity assays: Utilization of this peptide-AMC conjugate is prevalent in quantitative studies of protease activity. Upon enzymatic cleavage at specific peptide bonds, the AMC group is released, resulting in a robust fluorescent signal that can be measured with high sensitivity. This enables researchers to monitor enzyme kinetics, determine substrate specificity, and compare the activity profiles of various proteolytic enzymes under controlled conditions. The mixed D/L configuration further allows for the assessment of protease stereoselectivity, which is particularly relevant in the characterization of non-conventional or engineered enzymes.
Inhibitor screening: The substrate's fluorogenic properties make it exceptionally well-suited for high-throughput screening of protease inhibitors. By providing a direct and quantifiable readout of enzymatic cleavage, it facilitates the identification and evaluation of potential inhibitory compounds in drug discovery or biochemical research pipelines. The presence of non-standard amino acid configurations increases the stringency of the assay, helping to discriminate between broad-spectrum and highly specific inhibitors, and enabling more nuanced analysis of inhibitor potency and selectivity.
Substrate specificity profiling: The defined sequence and stereochemical diversity of the peptide chain enable in-depth studies of enzyme-substrate interactions. Researchers can employ this compound to map the substrate recognition preferences of various proteases, including those with altered or engineered specificity. Such profiling is instrumental in understanding the molecular determinants of enzyme function, guiding the rational design of tailored substrates or inhibitors, and supporting the development of biocatalytic processes.
Peptidase resistance studies: The incorporation of D-amino acids within the peptide backbone imparts enhanced resistance to degradation by most endogenous peptidases. This property is particularly valuable for investigating the stability of peptide substrates in complex biological matrices, such as cell lysates or tissue extracts. By comparing the degradation rates of this substrate to those of all-L analogs, researchers can gain insights into the mechanisms of peptide stability and the influence of stereochemistry on proteolytic susceptibility.
Assay development and optimization: The fluorescence-based detection enabled by the AMC tag, combined with the unique sequence characteristics of the peptide, supports the development of robust and sensitive enzymatic assays. Researchers can fine-tune assay conditions, such as buffer composition, temperature, and cofactor requirements, to maximize signal-to-noise ratios and reproducibility. This compound is thus a valuable resource for laboratories seeking to establish or refine protocols for protease activity measurement, inhibitor evaluation, or substrate screening in both academic and industrial settings.
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