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L-Pyroglutamic acid 4-nitroanilide

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Substrate for pyrrolidonylpeptidase.

Category

Cyclic Amino Acids

Catalog number

BAT-005606

CAS number

66642-35-1

Molecular Formula

C11H11N3O4

Molecular Weight

249.22

IUPAC Name

(2S)-N-(4-nitrophenyl)-5-oxopyrrolidine-2-carboxamide

Synonyms

L-Pyr-pNA

Appearance

Light yellow crystalline powder

Purity

≥ 99% (HPLC)

Density

1.451 g/cm3

Melting Point

216-222 °C

Boiling Point

627.1 °C

Storage

Store at 2-8°C

InChI

InChI=1S/C11H11N3O4/c15-10-6-5-9(13-10)11(16)12-7-1-3-8(4-2-7)14(17)18/h1-4,9H,5-6H2,(H,12,16)(H,13,15)/t9-/m0/s1

InChI Key

HGNBEWLBSCSJGV-VIFPVBQESA-N

Canonical SMILES

C1CC(=O)NC1C(=O)NC2=CC=C(C=C2)[N+](=O)[O-]

L-Pyroglutamic acid 4-nitroanilide is a chemical compound derived from the combination of L-Pyroglutamic acid and 4-nitroaniline. It is formed through a peptide bond linkage, incorporating the 4-nitroanilide group to L-Pyroglutamic acid. This compound serves as a useful intermediate in organic synthesis and has unique chemical properties due to the presence of the nitro group. The structure of L-Pyroglutamic acid 4-nitroanilide offers opportunities for targeted modifications, making it valuable in various research and industrial applications.

One key application of L-Pyroglutamic acid 4-nitroanilide is in the development of fluorescent probes for biochemical research. The 4-nitroanilide group can be used to create compounds that emit fluorescence under specific conditions, making it useful in studying enzyme activity, protein-protein interactions, and cellular processes. By incorporating L-Pyroglutamic acid, researchers can also explore the role of pyroglutamate in various biological systems. These fluorescent probes are essential tools in molecular biology and drug discovery.

L-Pyroglutamic acid 4-nitroanilide is also utilized in the synthesis of bioactive peptides and peptoid analogs. The combination of L-Pyroglutamic acid with the 4-nitroanilide group enables the creation of peptides with enhanced stability and specific binding properties. This makes it valuable in medicinal chemistry, particularly for the development of compounds with targeted therapeutic effects. Its unique structure allows researchers to design peptides with desired biological activities, which can be applied in treatments for cancer, neurodegenerative diseases, and infections.

In the field of analytical chemistry, L-Pyroglutamic acid 4-nitroanilide is used as a reagent for detecting and quantifying amino acids and peptides in complex biological samples. The compound's reactivity with primary amines makes it suitable for use in assays that require high sensitivity and specificity. This application is important for proteomics and the study of amino acid metabolism, where accurate detection of specific amino acids or peptides is crucial for understanding cellular functions and disease mechanisms.

L-Pyroglutamic acid 4-nitroanilide also finds application in materials science, specifically in the development of functional polymers. The compound’s ability to form stable linkages allows it to be incorporated into polymer networks, providing materials with improved mechanical properties and bioactivity. These polymers can be used in drug delivery systems, tissue engineering, and other biocompatible applications where controlled release of bioactive molecules is required. Its incorporation into polymer systems enhances the performance of materials in various biomedical applications.

1. Aminopeptidases in Caenorhabditis elegans and Panagrellus redivivus: detection using peptide and non-peptide substrates

E P Masler J Helminthol. 2002 Mar;76(1):45-52. doi: 10.1079/JOH200193.

Aminopeptidase activities were detected in extracts of the free-living nematodes Caenorhabditis elegans and Panagrellus redivivus using the aminoacyl substrate L-alanine-4-nitroanilide. The activities exhibited similarities in Km (C. elegans = 2.22 mM; P. redivivus = 2.09 mM) and specific activity (C. elegans = 1.38 +/- 0.43 mAU min(-1) x g(-1); P. redivivus, 1.23 +/- 0.18m AU min(-1) microg(-1). Each is inhibited competitively by amastatin (C. elegans IC50 = 0.46 microM; P. redivivus IC50 = 15.90 microM) and non-competitively by leuhistin (C. elegans IC50 = 3.00 microM; P. redivivus IC50 = 37.35 microM). The bioactive peptides adipokinetic hormone and substance P decrease the apparent aminopeptidase activities of each extract suggesting that the peptides compete with the Ala-pNA as substrates. With each extract, adipokinetic hormone appeared to be the more effective substrate. Digestion of adipokinetic hormone by C. elegans and P. redivivus extracts in the presence and absence of 1 mM amastatin produced distinct chromatographic profiles that suggest different digestion patterns for the two species. However, amastatin had clear effects on chromatographic profiles from each species indicating that an aminopeptidase is involved in the digestion of the peptide substrates. The data presented indicate that extracts of free-living nematodes are capable of metabolizing peptide hormones, and that this metabolism involves substrate-selective aminopeptidases.

2. Metabolites Associated With Malnutrition in the Intensive Care Unit Are Also Associated With 28-Day Mortality

Kris M Mogensen, et al. JPEN J Parenter Enteral Nutr. 2017 Feb;41(2):188-197. doi: 10.1177/0148607116656164. Epub 2016 Jul 19.

Background: We hypothesized that metabolic profiles would differ in critically ill patients with malnutrition relative to those without. Materials and methods: We performed a prospective cohort study on 85 adult patients with systemic inflammatory response syndrome or sepsis admitted to a 20-bed medical intensive care unit (ICU) in Boston. We generated metabolomic profiles using gas and liquid chromatography and mass spectroscopy. We followed this by logistic regression and partial least squares discriminant analysis to identify individual metabolites that were significant. We then interrogated the entire metabolomics profile using metabolite set enrichment analysis and network model construction of chemical-protein target interactions to identify groups of metabolites and pathways that were differentiates in patients with and without malnutrition. Results: Of the cohort, 38% were malnourished at admission to the ICU. Metabolomic profiles differed in critically ill patients with malnutrition relative to those without. Ten metabolites were significantly associated with malnutrition ( P < .05). A parsimonious model of 5 metabolites effectively differentiated patients with malnutrition (AUC = 0.76), including pyroglutamine and hypoxanthine. Using pathway enrichment analysis, we identified a critical role of glutathione and purine metabolism in predicting nutrition. Nutrition status was associated with 28-day mortality, even after adjustment for known phenotypic variables associated with ICU mortality. Importantly, 7 metabolites associated with nutrition status were also associated with 28-day mortality. Conclusion: Malnutrition is associated with differential metabolic profiles early in critical illness. Common to all of our metabolome analyses, glutathione and purine metabolism, which play principal roles in cellular redox regulation and accelerated tissue adenosine triphosphate degradation, respectively, were significantly altered with malnutrition.

3. L-Pyroglutamyl-L-phenylalanyl-L-leucine-p-nitroanilide--a chromogenic substrate for thiol proteinase assay

Filippova IYu, E N Lysogorskaya, E S Oksenoit, G N Rudenskaya, V M Stepanov Anal Biochem. 1984 Dec;143(2):293-7. doi: 10.1016/0003-2697(84)90665-1.

L-Pyroglutamyl-L-phenylalanyl-L-leucine-p-nitroanilide (PFLNA)--a convenient chromogenic substrate for assay of thiol proteinases papain, ficin, and bromelain--was prepared by enzymatic synthesis with chymotrypsin as a catalyst. The thiol proteinases hydrolyze PFLNA with the liberation of p-nitroaniline, estimated spectrophotometrically by its absorbance at 410 nm. The phenylalanine residue in the P2 position of PFLNA meets the specificity demands of thiol proteinases. The following values of Km were found for PFLNA hydrolysis: by papain, 0.34 mM; by ficin, 0.43 mM; by bromelain, 0.30 mM. This substrate was successfully applied to monitor thiol proteinase affinity chromatography on bacitracin-Sepharose, which resulted in a 2- to 4-fold purification from commercial preparations.