MC-Val-Ala-PAB-PNP integrates a modular linker with chromogenic functionality, aiding kinetic monitoring of cleavage reactions. Valine and alanine establish a hydrophobic motif that influences enzyme recognition. The PNP leaving group enables sensitive detection in biochemical assays. Applications include protease characterization, prodrug model design, and reaction-mechanism studies.
CAT No: R2330
CAS No:1639939-40-4
Synonyms/Alias:MC-Val-Ala-PAB-PNP;1639939-40-4;[4-[[(2S)-2-[[(2S)-2-[6-(2,5-Dioxopyrrol-1-yl)hexanoylamino]-3-methylbutanoyl]amino]propanoyl]amino]phenyl]methyl (4-nitrophenyl) carbonate;4-((S)-2-((S)-2-(6-(2,5-Dioxo-2,5-dihydro-1H-pyrrol-1-yl)hexanamido)-3-methylbutanamido)propanamido)benzyl (4-nitrophenyl) carbonate;MFCD32220341;Mal-Val-Ala-PAB-PNP;SCHEMBL16285134;{4-[(2S)-2-[(2S)-2-[6-(2,5-dioxo-2,5-dihydro-1H-pyrrol-1-yl)hexanamido]-3-methylbutanamido]propanamido]phenyl}methyl 4-nitrophenyl carbonate;AKOS040743576;BP-28055;DA-70018;MS-30966;PD171021;HY-135975;CS-0119076;F75033;6-maleimidohexanoyl-valyl-alanyl-(4-aminobenzyl)-(4-nitrophenyl)-carbonate;{4-[(2S)-2-[(2S)-2-[6-(2,5-dioxopyrrol-1-yl)hexanamido]-3-methylbutanamido]propanamido]phenyl}methyl 4-nitrophenyl carbonate;
MC-Val-Ala-PAB-PNP is a synthetic peptide-based substrate widely utilized in biochemical research, particularly in the study of protease activity and enzyme kinetics. As a derivative of the well-established Val-Ala dipeptide motif, this compound is engineered with a para-aminobenzyl (PAB) linker and a p-nitrophenyl (PNP) leaving group, enabling sensitive detection of enzymatic cleavage events. Its modular structure and chromogenic properties make it highly valuable for investigating the specificity and catalytic behavior of proteolytic enzymes in diverse biological and analytical settings.
Enzyme Activity Assays: In protease research, MC-Val-Ala-PAB-PNP serves as a reliable chromogenic substrate for quantifying enzyme activity. Upon enzymatic cleavage, the PNP moiety is released, producing a measurable colorimetric signal that can be precisely monitored using spectrophotometric methods. This enables detailed kinetic analyses of serine, cysteine, or other proteases with affinity for the Val-Ala recognition sequence, facilitating studies on substrate specificity, catalytic efficiency, and inhibitor screening.
High-Throughput Screening: The compound's robust and easily detectable colorimetric response makes it particularly suitable for high-throughput screening platforms. Researchers employ it to rapidly assess large libraries of enzyme variants, potential inhibitors, or activators, streamlining the identification of compounds that modulate protease function. Its compatibility with microplate-based assays supports efficient data acquisition and comparative analysis across multiple experimental conditions.
Enzyme Mechanism Studies: MC-Val-Ala-PAB-PNP is instrumental in elucidating the mechanistic details of proteolytic cleavage. By providing a defined substrate with a quantifiable reaction endpoint, it allows investigators to dissect catalytic mechanisms, investigate transition states, and characterize intermediate formation. This contributes to a deeper understanding of enzyme function at the molecular level, supporting the rational design of targeted inhibitors or modified enzymes.
Substrate Specificity Profiling: The modular design of this peptide substrate enables precise investigation of protease substrate preferences. By comparing cleavage rates with related dipeptide sequences or modified analogs, researchers can map the substrate recognition patterns and binding site requirements of target enzymes. This information is essential for both fundamental enzymology and the development of selective probes or inhibitors for specific protease families.
Analytical Method Development: The chromogenic properties and defined cleavage chemistry of MC-Val-Ala-PAB-PNP support its use in the development and validation of analytical assays for protease detection and quantification. It is frequently incorporated into standardized protocols for enzyme quality control, activity measurement in recombinant protein production, or monitoring protease contamination in bioprocessing workflows. Its performance characteristics contribute to reproducible, sensitive, and scalable assay formats in both academic and industrial laboratories.
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