Ac-Arg-Gly-Lys(Ac)-AMC integrates an acetylated motif with a fluorogenic AMC unit for precise enzymatic-cleavage detection. Charged residues promote solubility and substrate binding. Researchers analyze its kinetic responses in fluorescence assays. Applications span protease profiling, substrate design, and mechanistic evaluation.
CAT No: R2333
CAS No:660846-97-9
Synonyms/Alias:Ac-Arg-Gly-Lys(Ac)-AMC;660846-97-9;(2S)-6-acetamido-2-[[2-[[(2S)-2-acetamido-5-(diaminomethylideneamino)pentanoyl]amino]acetyl]amino]-N-(4-methyl-2-oxochromen-7-yl)hexanamide;Ac-Arg-Gly-Lys(Ac)-AMC trifluoroacetate salt;Ac-Arg-Gly-Lys(Ac)-MCA;Ac-KGLGK(Ac)-AMC;BDBM19150;HY-P2462;Ac-RGK(Ac)-AMC trifluoroacetate salt;AKOS040755413;DA-60709;FA110598;CS-0134449;G13476;N-Acetyl-Arg-Gly-Lys(acetyl)-7-amido-4-methylcoumarin trifluoroacetate salt;
Ac-Arg-Gly-Lys(Ac)-AMC is a synthetic peptide substrate featuring an N-terminal acetylated arginine-glycine sequence, an acetylated lysine residue, and a C-terminal 7-amino-4-methylcoumarin (AMC) fluorogenic group. Designed for advanced biochemical studies, this compound is particularly relevant in the investigation of lysine acetylation-dependent enzymatic processes. Its structure enables researchers to monitor specific protease and deacetylase activities by exploiting the fluorescence properties of the AMC moiety, which is released upon enzymatic cleavage. The substrate's modular design and site-specific modifications make it a powerful tool for elucidating the function and specificity of enzymes involved in post-translational modification pathways.
Enzyme Activity Assays: As a fluorogenic peptide substrate, Ac-Arg-Gly-Lys(Ac)-AMC is widely used to quantify the activity of lysine deacetylases, such as histone deacetylases (HDACs) and sirtuins, in vitro. Upon enzymatic removal of the acetyl group from the lysine residue, the peptide becomes susceptible to proteolytic cleavage, resulting in the liberation of AMC and a measurable fluorescence signal. This sensitive readout allows for precise kinetic analysis of deacetylase activity, facilitating the characterization of enzyme specificity, catalytic efficiency, and the effects of small-molecule modulators.
Epigenetic Research: The acetylated lysine within the peptide mimics physiologically relevant post-translational modifications found in histones and other nuclear proteins. Researchers employ this substrate to probe the molecular mechanisms underlying chromatin remodeling and gene regulation, using the fluorescence-based assay to monitor the removal of acetyl groups in real time. This application provides critical insights into the dynamic interplay between acetylation and gene expression, supporting the development of novel epigenetic modulators and the study of chromatin-associated protein complexes.
Inhibitor Screening: The robust and quantifiable fluorescence response generated by AMC release makes this peptide an ideal candidate for high-throughput screening of deacetylase inhibitors. By measuring changes in fluorescence intensity, scientists can rapidly assess the potency and selectivity of candidate compounds, accelerating the discovery and optimization of novel enzyme inhibitors. This approach is particularly valuable in early-stage drug discovery and chemical biology, where rapid, reliable assay formats are essential for lead identification and structure-activity relationship studies.
Protease Substrate Specificity: Beyond deacetylase assays, Ac-Arg-Gly-Lys(Ac)-AMC serves as a model substrate for evaluating the specificity of proteases that recognize acetylated lysine motifs. By systematically varying the peptide sequence or acetylation status, researchers can dissect the substrate preferences of different proteolytic enzymes, shedding light on the molecular determinants of substrate recognition and catalysis. Such studies inform the rational design of selective substrates and inhibitors for diverse protease families.
Assay Development and Optimization: The modular nature of this fluorogenic peptide enables its integration into a variety of assay platforms, including microplate-based fluorescence assays, kinetic studies, and multiplexed screening formats. Its predictable response to enzymatic modification makes it a valuable standard for optimizing assay conditions, validating detection systems, and benchmarking the performance of new analytical methodologies. By providing a reliable and sensitive means to monitor enzyme activity, the compound supports the advancement of biochemical assay technology and the broader field of enzymology research.
1. Emerging applications of nanotechnology for diagnosis and therapy of disease: a review
4. The spatiotemporal control of signalling and trafficking of the GLP-1R
If you have any peptide synthesis requirement in mind, please do not hesitate to contact us at . We will endeavor to provide highly satisfying products and services.
Creative Peptides is a trusted CDMO partner specializing in high-quality peptide synthesis, conjugation, and manufacturing under strict cGMP compliance. With advanced technology platforms and a team of experienced scientists, we deliver tailored peptide solutions to support drug discovery, clinical development, and cosmetic innovation worldwide.
From custom peptide synthesis to complex peptide-drug conjugates, we provide flexible, end-to-end services designed to accelerate timelines and ensure regulatory excellence. Our commitment to quality, reliability, and innovation has made us a preferred partner across the pharmaceutical, biotechnology, and personal care industries.
Read More