37159-97-0

Usage

Uses

Used in Biochemical Research:
L-PROLINE-(4-3H(N)) serves as a vital tool in biochemical research, where it is used as a tracer molecule to study the metabolic pathways and mechanisms involving L-proline. The radiolabeled nature of the compound allows researchers to monitor its incorporation into proteins and other biomolecules, providing a deeper understanding of amino acid metabolism.
Used in Pharmacological Research:
In pharmacological studies, L-PROLINE-(4-3H(N)) is utilized as a radiolabeled probe to investigate the distribution and behavior of proline in living organisms. This helps in assessing the bioavailability, metabolism, and potential interactions of proline-containing drugs or compounds with biological systems.
Used in Protein Synthesis Studies:
L-PROLINE-(4-3H(N)) is employed in research focused on protein synthesis, where it acts as a labeled substrate to observe the incorporation of proline into newly synthesized proteins. This application aids in elucidating the kinetics and regulation of protein synthesis at the molecular level.
Used in Cellular Process Investigations:
L-PROLINE-(4-3H(N)) is used as a research reagent to explore various cellular processes that involve L-proline. The radiolabeled compound can reveal details about the role of proline in cell signaling, enzyme activity, and other critical cellular functions.
Used in Metabolic Pathway Analysis:
In the field of metabolic pathway analysis, L-PROLINE-(4-3H(N)) is applied to map out the specific routes through which proline is metabolized within cells. This can contribute to the identification of key enzymes and regulatory steps in proline metabolism.
Used in Radiotracer Kinetics:
L-PROLINE-(4-3H(N)) is utilized in the study of radiotracer kinetics, where its radioactive label allows for the measurement of the compound's uptake, distribution, metabolism, and excretion. This information is crucial for understanding the pharmacokinetics of proline and related compounds in biological systems.

InChI:InChI=1/C5H9NO2/c7-5(8)4-2-1-3-6-4/h4,6H,1-3H2,(H,7,8)/t4-/m0/s1

Upstream product

• 6829-40-9 aminomalonic acid diethyl ester 
• 617-65-2 Glutamic acid 
• 6326-44-9 diethyl 2-formylaminomalonate 
• 109-70-6 1.3-chlorobromopropane 
• 55514-92-6 N-nitrosoproline 
• 79068-39-6 Natrium-(3-chlor-1-pyrrolin-2-carboxylat) 
• 75-05-8 acetonitrile 
• 1148-11-4 N-carbobenzyloxyproline 
• 2577-48-2 methyl (2S)-pyrrolidine carboxylate 
• 7647-01-0 hydrogenchloride 
• 858449-85-1 1-((Ξ)-2-hydroxy-4-methyl-valeryl)-DL-proline amide 
• 70-26-8 L-ornithine 
• 372-75-8 Citrulline 
• 7664-93-9 sulfuric acid 

Downstream Products

• 119910-72-4 1,2,3,3aα,4β,6,7,8,8aα,8bα-decahydro-2-phenyl-4-(2-pyridyl)pyrrolo<3,4-a>pyrrolizine-1,3-dione 
• 119910-72-4 1,2,3,3aα,4α,6,7,8,8aβ,8bα-decahydro-2-phenyl-4-(2-pyridyl)pyrrolo<3,4-a>pyrrolizine-1,3-dione 
• 18877-34-4 1,2,3,11a-tetrahydro-10H-benzo[e]pyrrolo[1,2-a][1,4]diazepine-5,11-dione 
• 7364-47-8 TMS-DL-Pro-OTMS 
• 137441-49-7 C₂₅H₃₄N₂O₃ 
• 73004-43-0 N-Carbethoxy-prolin 
• 108286-48-2 3-Methyl-1-phenyl-6,7-dihydro-5H-pyrrolizine-2-carbonitrile 
• 108286-45-9 3-Methyl-2-phenyl-6,7-dihydro-5H-pyrrolizine-1-carboxylic acid methyl ester 
• 108286-44-8 3-Methyl-1-phenyl-6,7-dihydro-5H-pyrrolizine-2-carboxylic acid methyl ester 
• 1074-79-9 N-Acetyl-DL-prolin 
• 103847-61-6 (2R,3S,7aR)-2,3-Bis-(4-nitro-phenyl)-hexahydro-pyrrolo[2,1-b]oxazole 
• 103847-61-6 (2S,3S,7aR)-2,3-Bis-(4-nitro-phenyl)-hexahydro-pyrrolo[2,1-b]oxazole 
• 80514-78-9 Trit-Pro-OH.Et2NH 
• 84969-62-0 Sodium; 1-(4-chloro-phenyl-diazenyl)-pyrrolidine-2-carboxylate 

Relevant academic research and scientific papers

Squamins C–F, four cyclopeptides from the seeds of Annona globiflora

Four cyclic octapeptides, squamins C–F, were isolated from the seeds of Annona globiflora Schltdl. These compounds share part of their amino acid sequence, -Pro-Met(O)-Tyr-Gly-Thr-, with previously reported squamins A and B. Their structures were determined using NMR spectroscopic techniques together with quantum mechanical calculations (QM-NMR), ESI-HRMS data and a modified version of Marfey's chromatographic method. All compounds showed cytotoxic activity against DU-145 (human prostate cancer) and HeLa (human cervical carcinoma) cell lines. Clearly, A. globiflora is an important source of bioactive molecules, which could promote the sustainable exploitation of this undervalued specie.

Direct monitoring of biocatalytic deacetylation of amino acid substrates by1H NMR reveals fine details of substrate specificity

Amino acids are key synthetic building blocks that can be prepared in an enantiopure form by biocatalytic methods. We show that thel-selective ornithine deacetylase ArgE catalyses hydrolysis of a wide-range ofN-acyl-amino acid substrates. This activity was revealed by1H NMR spectroscopy that monitored the appearance of the well resolved signal of the acetate product. Furthermore, the assay was used to probe the subtle structural selectivity of the biocatalyst using a substrate that could adopt different rotameric conformations.

MODIFIED INTERLEUKIN-7 PROTEINS AND USES THEREOF

Provided are a modified IL-7 polypeptide and a fusion protein containing the modified IL-7 polypeptide. The fusion protein of the modified IL-7 includes: a first domain containing an interleukin-7 polypeptide; a second domain containing an oligopeptide having 1 to 10 amino acid residues (with proviso that the second domain excludes the oligopeptide consisting of methionine and/or glycine); and (c) a third domain which prolongs the half-life of the IL-7 fusion protein. The modified IL-7 polypeptide is composed of the (a) first domain and the (b) second domain. The modified IL-7 polypeptide and the fusion protein are expressed in a higher yield than the wild-type IL-7 and shows increased stability.

COMPOSITIONS AND METHODS FOR USING FIXED BIOLOGICAL SAMPLES IN PARTITION-BASED ASSAYS

The present disclosure provides compositions and methods for using fixed biological samples in partition-based assays. In at least one embodiment, the disclosure provides a composition comprising a fixed biological sample and an un-fixing agent contained in a partition, such as a discrete droplet. In some embodiments, the disclosure provides un-fixing agent compounds capable of catalytically cleaving crosslinks in fixed biological samples, particularly crosslinked nucleic acids, such as RNA.

Leveraging Peptaibol Biosynthetic Promiscuity for Next-Generation Antiplasmodial Therapeutics

Malaria remains a worldwide threat, afflicting over 200 million people each year. The emergence of drug resistance against existing therapeutics threatens to destabilize global efforts aimed at controlling Plasmodium spp. parasites, which is expected to leave vast portions of humanity unprotected against the disease. To address this need, systematic testing of a fungal natural product extract library assembled through the University of Oklahoma Citizen Science Soil Collection Program has generated an initial set of bioactive extracts that exhibit potent antiplasmodial activity (EC50 25 μM, selectivity index > 250). The unique chemodiversity afforded by these fungal isolates serves to unlock new opportunities for translating peptaibols into a bioactive scaffold worthy of further development.

Isolation, Structure Determination, and Total Synthesis of Hoshinoamide C, an Antiparasitic Lipopeptide from the Marine Cyanobacterium Caldora penicillata

Hoshinoamide C (1), an antiparasitic lipopeptide, was isolated from the marine cyanobacterium Caldora penicillata. Its planar structure was elucidated by spectral analyses, mainly 2D NMR, and the absolute configurations of the α-amino acid moieties were determined by degradation reactions followed by chiral-phase HPLC analyses. To clarify the absolute configuration of an unusual amino acid moiety, we synthesized two possible diastereomers of hoshinoamide C and determined its absolute configuration based on a comparison of their spectroscopic data with those of the natural compound. Hoshinoamide C (1) did not exhibit any cytotoxicity against HeLa or HL60 cells at 10 μM, but inhibited the growth of the parasites responsible for malaria (IC50 0.96 μM) and African sleeping sickness (IC50 2.9 μM).

Genomics-driven discovery of a new cyclodepsipeptide from the guanophilic fungusAmphichorda guana

Two potential non-ribosomal peptide synthetases (NRPSs) were identified in the genome of a guanophilic fungusAmphichorda guanaby bioinformatics analysis and gene knockout experiments. Liquid chromatography coupled with mass spectrometry (LC-MS) guided isolation led to the discovery of a new cyclodepsipeptide isaridin H (1) and seven known analogs, desmethylisaridin E (2), isaridin E (3), isariin A (4), iso-isariin B (5), iso-isariin D (6), isariin E (7), and nodupetide (8). The absolute configuration of isaridin H (1) was achieved by Marfey's method. Isaridin H (1) showed significant antifungal activity againstBotrytis cinereaandAlternaria solani.

Komesuamide and odopenicillatamide, two linear lipopeptides from the marine cyanobacterium Caldora penicillata

The linear lipopeptides komesuamide (1) and odopenicillatamide (2) were isolated from Caldora penicillata a marine cyanobacterium collected in Okinawa. The structures of these compounds were established by spectroscopic analyses, and the absolute configurations were determined by HPLC analyses of the acid hydrolysates. Both compounds showed glucose uptake activity at 40 μM in cultured L6 myotubes.

Motobamide, an Antitrypanosomal Cyclic Peptide from a Leptolyngbya sp. Marine Cyanobacterium

Motobamide (1), a new cyclic peptide containing a C-prenylated cyclotryptophan residue, was isolated from a marine Leptolyngbya sp. cyanobacterium. Its planar structure was established by spectroscopic and MS/MS analyses. The absolute configuration was elucidated based on a combination of chemical degradations, chiral-phase HPLC analyses, spectroscopic analyses, and computational chemistry. Motobamide (1) moderately inhibited the growth of bloodstream forms of Trypanosoma brucei rhodesiense (IC50 2.3 μM). However, it exhibited a weaker cytotoxicity against normal human cells (IC50 55 μM).

Argicyclamides A-C Unveil Enzymatic Basis for Guanidine Bis-prenylation

Guanidine prenylation is an outstanding modification in alkaloid and peptide biosynthesis, but its enzymatic basis has remained elusive. We report the isolation of argicyclamides, a new class of cyanobactins with unique mono- and bis-prenylations on guanidine moieties, from Microcystis aeruginosa NIES-88. The genetic basis of argicyclamide biosynthesis was established by the heterologous expression and in vitro characterization of biosynthetic enzymes including AgcF, a new guanidine prenyltransferase. This study provides important insight into the biosynthesis of prenylated guanidines and offers a new toolkit for peptide modification.