Boc-Val-Leu-Gly-Arg-pNA pairs a protected peptide sequence with a chromogenic leaving group for monitoring cleavage reactions. Valine, leucine, and glycine shape hydrophobic and flexible domains, influencing recognition by enzymes. Arginine contributes strong charge complementarity. Research uses include protease profiling, kinetic measurements, and synthetic method development.
CAT No: R2456
CAS No:68223-95-0
Synonyms/Alias:Boc-Val-Leu-Gly-Arg-pNA;68223-95-0;tert-butyl N-[(2S)-1-[[(2S)-1-[[2-[[(2S)-5-(diaminomethylideneamino)-1-(4-nitroanilino)-1-oxopentan-2-yl]amino]-2-oxoethyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]carbamate;Boc-Val-Leu-Gly-Arg-pNA acetate salt;SCHEMBL1925288;FB110715;tert-Butyl ((6S,12S,15S)-1,1-diamino-12-isobutyl-16-methyl-6-((4-nitrophenyl)carbamoyl)-8,11,14-trioxo-2,7,10,13-tetraazaheptadec-1-en-15-yl)carbamate;
Boc-Val-Leu-Gly-Arg-pNA is a synthetic peptide substrate that integrates the N-terminal tert-butyloxycarbonyl (Boc) protecting group with a tetrapeptide sequence (Valine-Leucine-Glycine-Arginine) and a para-nitroanilide (pNA) chromogenic tag at the C-terminus. This compound is widely employed in biochemical research as a model substrate for serine proteases, particularly those with trypsin-like specificity. Its modular peptide structure and chromogenic reporter enable precise investigation of enzyme activity, substrate specificity, and proteolytic mechanisms. The presence of the pNA moiety allows for direct colorimetric detection of enzymatic cleavage, making it a valuable tool in both fundamental enzymology and applied assay development.
Enzyme Activity Assays: As a chromogenic peptide substrate, Boc-Val-Leu-Gly-Arg-pNA is extensively utilized in quantitative enzyme assays to measure the activity of serine proteases such as trypsin, thrombin, and related enzymes. Upon enzymatic hydrolysis at the arginine-pNA bond, the release of para-nitroaniline yields a measurable yellow color, facilitating real-time monitoring of proteolytic activity via spectrophotometric analysis. This enables researchers to determine kinetic parameters, compare enzyme variants, and assess inhibitor potency under controlled laboratory conditions.
Substrate Specificity Profiling: The defined sequence of this tetrapeptide, featuring a basic arginine residue at the P1 position, supports its application in substrate specificity studies. By systematically varying peptide substrates and analyzing cleavage efficiency, scientists can elucidate the substrate preferences of target proteases. Data generated using this compound contribute to mapping protease recognition motifs and refining our understanding of enzyme-substrate interactions at the molecular level.
Inhibitor Screening: Boc-Val-Leu-Gly-Arg-pNA serves as a reliable substrate for high-throughput screening of protease inhibitors. Its chromogenic readout enables rapid evaluation of compound libraries for inhibitory effects on serine protease activity, streamlining the identification and characterization of lead molecules. Such screening platforms are essential for both academic research and early-stage drug discovery, providing robust, reproducible data on inhibitor efficacy.
Method Validation and Quality Control: The substrate's well-characterized cleavage properties make it an important standard in the validation and calibration of enzymatic assay protocols. Laboratories employ this compound to verify assay sensitivity, dynamic range, and reproducibility, ensuring consistent performance across experimental runs. Its use in quality control workflows supports the standardization of protease activity measurements in both research and industrial environments.
Protease Mechanism Studies: The modular design of Boc-Val-Leu-Gly-Arg-pNA facilitates mechanistic investigations into proteolytic cleavage events. By monitoring reaction rates and product formation, researchers can dissect catalytic mechanisms, probe active site function, and evaluate the effects of mutations or environmental factors on enzyme behavior. Such mechanistic insights are fundamental to advancing our knowledge of protease biology and informing the rational design of enzyme modulators.
1. The spatiotemporal control of signalling and trafficking of the GLP-1R
2. Immune-awakening Saccharomyces-inspired nanocarrier for oral target delivery to lymph and tumors
3. Immune responses to homocitrulline-and citrulline-containing peptides in rheumatoid arthritis
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