D-Ile-Pro-Arg p-nitroanilide dihydrochloride combines a stereochemically altered tripeptide with a chromogenic reporter for cleavage assessment. The nitroanilide group enables precise spectroscopic monitoring. Researchers evaluate enzymatic specificity using its distinct reactivity. Applications include kinetic profiling, protease screening, and mechanistic studies.
CAT No: R2694
CAS No:96323-41-0
Synonyms/Alias:D-Ile-Pro-Arg p-nitroanilide dihydrochloride;96323-41-0;(2S)-1-[(2R,3R)-2-amino-3-methylpentanoyl]-N-[(2S)-5-(diaminomethylideneamino)-1-(4-nitroanilino)-1-oxopentan-2-yl]pyrrolidine-2-carboxamide;dihydrochloride;D-Ile-pro-arg p-nitroanilide*dihydrochlo ride;SCHEMBL6673589;DTXSID20595347;NAANFMDBMZZFRD-CYTOJJGESA-N;D-Ile-Pro-Arg p-nitroanilide dihydrochloride, >=95% (HPLC);(S)-1-((2R,3R)-2-amino-3-methylpentanoyl)-N-((S)-5-guanidino-1-(4-nitrophenylamino)-1-oxopentan-2-yl)pyrrolidine-2-carboxamide dihydrochloride;D-Isoleucyl-L-prolyl-N~5~-(diaminomethylidene)-N-(4-nitrophenyl)-L-ornithinamide--hydrogen chloride (1/2);
D-Ile-Pro-Arg p-nitroanilide dihydrochloride is a synthetic peptide substrate widely utilized in biochemical and enzymological research. Structurally, it consists of a sequence of D-isoleucine, proline, and arginine, conjugated to a p-nitroanilide chromogenic group, and is supplied as the dihydrochloride salt to enhance solubility and stability. The incorporation of the D-isomer at the N-terminus imparts resistance to nonspecific proteolytic degradation, while the p-nitroanilide moiety enables colorimetric detection upon enzymatic cleavage. This compound is particularly valued for its role in the study of protease specificity, kinetic analysis, and the development of enzyme assays in both academic and industrial research settings.
Enzyme substrate assays: As a chromogenic peptide substrate, D-Ile-Pro-Arg p-nitroanilide dihydrochloride is extensively employed in the quantitative measurement of serine protease activity, especially those with trypsin-like or arginine-specific cleavage preferences. Upon enzymatic hydrolysis, the release of p-nitroaniline generates a measurable color change, allowing for rapid and sensitive spectrophotometric analysis. This property supports high-throughput screening of protease inhibitors, enzyme kinetics studies, and the characterization of substrate specificity in purified enzyme preparations or complex biological samples.
Protease characterization: The sequence and stereochemistry of this peptide substrate facilitate detailed investigation of protease substrate recognition and catalytic mechanisms. Researchers utilize it to distinguish between endopeptidase and exopeptidase activity, as well as to assess the influence of D-amino acid residues on enzyme selectivity. Such studies provide crucial insights into enzyme-substrate interactions, inform rational inhibitor design, and support the development of novel biochemical tools for protease profiling.
Biochemical pathway analysis: By enabling precise monitoring of proteolytic activity, this synthetic substrate aids in elucidating the roles of specific serine proteases within broader metabolic or signaling pathways. Its application extends to dissecting protease cascades in cell extracts, tissue homogenates, or reconstituted systems, where the controlled release of the chromophore serves as a reliable indicator of enzymatic function. This approach is instrumental in identifying regulatory checkpoints, mapping protease networks, and validating functional hypotheses in proteolysis research.
Assay development and optimization: The robust chromogenic response and defined cleavage site of D-Ile-Pro-Arg p-nitroanilide dihydrochloride make it an ideal standard for the development and calibration of new protease assays. Laboratories leverage its properties to optimize assay conditions, determine detection limits, and validate reproducibility across different platforms. Its use supports the establishment of standardized protocols for enzyme activity measurement, facilitating cross-study comparisons and methodological consistency.
Analytical quality control: In industrial and academic laboratories, this peptide substrate is also applied as a quality control reagent for verifying the functional activity of protease preparations or screening for contaminating enzymatic activities in biochemical formulations. The sensitive colorimetric readout enables rapid assessment of batch-to-batch consistency, stability testing, and troubleshooting of enzyme-based processes, ensuring reliable performance in downstream applications.
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