H-Gly-Pro-pNA.HCl has been used as a substrate in dipeptidyl peptidase-IV (DPP-IV) enzyme assay. It has also been used to determine DPP-IV inhibitory activity.
CAT No: 10-101-345
CAS No:103213-34-9
Synonyms/Alias:103213-34-9;GP-pNA, Chromogenic Substrate;Gly-Pro p-nitroanilide hydrochloride;DTXSID90585159;1-(2-aminoacetyl)-N-(4-nitrophenyl)pyrrolidine-2-carboxamide;hydrochloride;Glycyl-N-(4-nitrophenyl)prolinamide--hydrogen chloride (1/1);H-Gly-Pro-pNA.HCl;H-Gly-Pro-pNA*hydrochloride;SCHEMBL20214289;DTXCID60535924;VBBFIBMVFSUUBP-UHFFFAOYSA-N;AKOS037645284;AS-59672;FG110792;D93308;Gly-Pro p-nitroanilide hydrochloride, >=99% (HPLC);1-(2-aminoacetyl)-N-(4-nitrophenyl)pyrrolidine-2-carboxamide hydrochloride;
Chemical Name:(2S)-1-(2-aminoacetyl)-N-(4-nitrophenyl)pyrrolidine-2-carboxamide;hydrochloride
H-Gly-Pro-pNA.HCl, also known as Glycyl-L-prolyl-4-nitroanilide hydrochloride, is a synthetic peptide substrate widely recognized for its utility in enzymatic assays, particularly those involving dipeptidyl peptidases and proline-specific proteases. Structurally, it consists of a dipeptide (glycine-proline) conjugated to a para-nitroanilide (pNA) chromogenic group, with the hydrochloride salt enhancing its solubility and handling. The compound's design allows for sensitive colorimetric detection of enzymatic activity, making it a valuable reagent in biochemical research focused on proteolytic mechanisms, substrate specificity, and enzyme kinetics. Its use supports a broad range of studies in enzymology, protein biochemistry, and molecular biology, where precise measurement and characterization of protease function are required.
Enzyme activity assays: As a chromogenic peptide substrate, H-Gly-Pro-pNA.HCl is extensively employed in the quantification and characterization of proline-specific peptidases, including dipeptidyl peptidase IV (DPP-IV) and prolyl endopeptidases. Upon enzymatic cleavage of the peptide bond, the release of 4-nitroaniline yields a yellow coloration measurable by spectrophotometry, enabling accurate determination of enzyme kinetics, substrate specificity, and inhibitor potency. This facilitates the detailed study of protease function in various biological contexts, supporting the development of new research tools and assay platforms.
Protease inhibitor screening: The compound serves as a reliable substrate in high-throughput screening assays for potential inhibitors of proline-specific proteases. By monitoring changes in chromogenic signal in the presence of candidate molecules, researchers can efficiently evaluate inhibitor efficacy and specificity. This application is particularly valuable in early-stage drug discovery and the development of molecular probes, where rapid and reproducible assessment of protease inhibition is essential for identifying promising lead compounds and elucidating mechanisms of action.
Substrate specificity profiling: H-Gly-Pro-pNA.HCl provides a defined and sensitive platform for mapping the substrate recognition profiles of various peptidases. By comparing the enzymatic turnover of this substrate with that of structurally related analogs, investigators can dissect the influence of peptide sequence and chemical modifications on enzyme selectivity. Such studies help clarify the structural determinants governing protease-substrate interactions, informing both basic enzymology and the rational design of targeted inhibitors or engineered enzymes.
Biochemical pathway elucidation: The use of this dipeptide-pNA conjugate extends to the investigation of metabolic and signaling pathways involving proline-containing peptides. By enabling precise measurement of peptidase activity under controlled conditions, it supports the exploration of proteolytic processing events in cellular extracts, tissue samples, or recombinant systems. Insights gained from these studies contribute to a deeper understanding of peptide turnover, regulatory mechanisms, and the physiological roles of specific protease families.
Analytical method development: Owing to its robust chromogenic response and well-characterized cleavage pattern, H-Gly-Pro-pNA.HCl is frequently incorporated into the development and optimization of analytical protocols for enzyme quantification. Its use in assay validation, calibration, and standard curve generation ensures reproducibility and comparability across experimental platforms. This enhances the reliability of data obtained in both academic and industrial research settings, supporting quality control and method standardization in protease-related investigations.
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