Dnp-PLGMWSR is a fluorogenic substrate for matrix metalloproteinase-2 (MMP-2) and MMP-9. The activity of MMP-2 and MMP-9 can be quantified by measuring tryptophan fluorescence that is unquenched upon peptide hydrolysis that removes the N-terminal dinitrophenol (Dnp) group.
CAT No: R1926
CAS No:135662-07-6
Synonyms/Alias:Dnp-PLGMWSR;135662-07-6;Dnp-PLGMWSR pound>>Dnp-Pro-Leu-Gly-Met-Trp-Ser-Arg-OH pound>>Matrix Metalloproteinase-2/Matrix Metalloproteinase-9 Fluorogenic Substrate I pound>>MMP-2/MMP-9 Fluorogenic Substrate I;Dnp-PLGMWSR (trifluoroacetate salt);HY-P2689;CS-0139728;(2S)-5-(diaminomethylideneamino)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-1-(2,4-dinitrophenyl)pyrrolidine-2-carbonyl]amino]-4-methylpentanoyl]amino]acetyl]amino]-4-methylsulfanylbutanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-3-hydroxypropanoyl]amino]pentanoic acid;
Chemical Name:(2S)-5-(diaminomethylideneamino)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-1-(2,4-dinitrophenyl)pyrrolidine-2-carbonyl]amino]-4-methylpentanoyl]amino]acetyl]amino]-4-methylsulfanylbutanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-3-hydroxypropanoyl]amino]pentanoic acid
Dnp-PLGMWSR is a synthetic peptide featuring an N-terminal dinitrophenyl (Dnp) modification, designed for advanced biochemical and proteomic research applications. As a custom-sequence peptide, it serves as a versatile molecular tool for investigating protein-protein interactions, substrate specificity, and enzymatic activity, particularly within the context of protease and peptidase studies. The presence of the Dnp group confers unique spectroscopic properties, enabling sensitive detection and quantification in a variety of assay formats. Its defined amino acid sequence and chemical stability make it suitable for experimental systems requiring precise molecular probes, including those exploring post-translational modifications or signal transduction pathways.
Enzyme substrate assays: Dnp-PLGMWSR is frequently employed as a chromogenic substrate in protease and peptidase activity assays. The Dnp moiety acts as a reliable spectroscopic reporter, allowing researchers to monitor enzyme-mediated cleavage events via absorbance or fluorescence changes. This feature is particularly valuable for kinetic studies, inhibitor screening, and enzyme characterization, enabling the quantification of catalytic efficiency and substrate specificity in both purified and complex biological samples.
Protease specificity profiling: The peptide sequence PLGMWSR provides a defined recognition motif for investigating the substrate preferences of various proteolytic enzymes. By incorporating the Dnp label, cleavage products can be readily detected, facilitating high-throughput analysis of enzyme-substrate interactions. This approach is instrumental in mapping protease cleavage sites, elucidating enzymatic mechanisms, and guiding the development of selective inhibitors or activity-based probes.
Peptide-based assay development: As a model peptide, Dnp-PLGMWSR supports the design and optimization of novel bioanalytical assays. Its sequence and chromophore enable the construction of sensitive detection platforms for monitoring enzymatic reactions or molecular interactions in vitro. The peptide can be adapted for use in microplate-based assays, HPLC, or mass spectrometry workflows, providing a robust standard for assay calibration and validation in research and industrial settings.
Signal transduction studies: The defined structure of Dnp-PLGMWSR makes it a valuable tool for dissecting signaling pathways involving proteolytic processing. Researchers employ this peptide to simulate or probe substrate cleavage events that regulate cellular signaling, protein maturation, or degradation. The ability to monitor cleavage with high sensitivity aids in clarifying the functional consequences of protease activity within complex biological networks.
Analytical method validation: Laboratories utilize Dnp-PLGMWSR as a reference material for validating peptide quantification and detection methods. Its well-characterized properties facilitate the assessment of analytical sensitivity, linearity, and reproducibility in spectrophotometric or chromatographic techniques. By serving as a benchmark for method development, the peptide supports rigorous quality control and enhances the reliability of peptide-based analytical workflows.
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