Selective ESI-MS detection of carbonyl containing compounds by aminooxyacetic acid immobilized on a resin

Kijewska, Monika; Koch, Tomasz; Waliczek, Mateusz; Konieczny, Andrzej; Stefanowicz, Piotr; Szewczuk, Zbigniew

doi:10.1016/j.aca.2021.338767

Cited by 3 publications

(7 citation statements)

References 49 publications

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“…In this review, we concentrated on our recent research to develop materials functionalized with different functional groups, in order to effectively enrich the sample into the selected analytes [7,8,19,29,80]. Despite the significant development of mass spectrometry coupled with liquid chromatography (LC-MS) and bioinformatics methods, the analysis of biological samples, in particular, the search and identification of new biomarkers present in trace amounts, is still a challenge [11,28,42,43].…”

Section: Discussion: Peptide Biosensors-advantages and Applicationsmentioning

confidence: 99%

“…We presented alternative methods of selective enrichment of compounds based on (i) reversible reactions, in which the compounds were released from the functionalized support in an unchanged form, such as deoxyfructosylated peptides [7] and (ii) irreversible reactions, in which the selectively bound analytes were released from the functionalized resin with an appropriate linker improving ionization properties during the LC-MS/MS analysis, such as carbonylated peptides [29], other compounds containing carbonyl group [8,29], peptides containing the SH group [19], and peptides containing the Tyr residue in sequence [80]. Moreover, the presented protocol may also be used for confirming the substrate specificity of executioner caspases, which suggests the applicability of the proposed methodology in the analysis of the on-bead substrate specificity and enzyme activity [169].…”

Section: Discussion: Peptide Biosensors-advantages and Applicationsmentioning

confidence: 99%

“…In our first approach, we merged the unique properties of hydroxylamine derivatives and the advantages of immobilizing reagents on a solid support, creating the functionalized resin derivatized with an aminooxy group that is ready for selective detection of carbonyl unit in peptides or steroids (testosterone derivatives, exemestane, methandrostenolone or methasterone) [29], which combined the enrichment and derivatization procedure of steroids into a single step protocol. For this purpose, we developed a method of synthesis of a functionalized resin (Fmoc-AOA-GRG-CMRR) containing (i) aminooxyacetic acid (AOA), selectively reacting with compounds containing a carbonyl group, and (ii) an arginine residue to increase the ionization efficiency of the compound during mass spectrometry analysis.…”

Section: Capturing Carbonylated Compoundsmentioning

confidence: 99%

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Veni, Vidi, Vici: Immobilized Peptide-Based Conjugates as Tools for Capture, Analysis, and Transformation

et al. 2022

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Analysis of peptide biomarkers of pathological states of the organism is often a serious challenge, due to a very complex composition of the cell and insufficient sensitivity of the current analytical methods (including mass spectrometry). One of the possible ways to overcome this problem is sample enrichment by capturing the selected components using a specific solid support. Another option is increasing the detectability of the desired compound by its selective tagging. Appropriately modified and immobilized peptides can be used for these purposes. In addition, they find application in studying the specificity and activity of proteolytic enzymes. Immobilized heterocyclic peptide conjugates may serve as metal ligands, to form complexes used as catalysts or analytical markers. In this review, we describe various applications of immobilized peptides, including selective capturing of cysteine-containing peptides, tagging of the carbonyl compounds to increase the sensitivity of their detection, enrichment of biological samples in deoxyfructosylated peptides, and fishing out of tyrosine–containing peptides by the formation of azo bond. Moreover, the use of the one-bead-one-compound peptide library for the analysis of substrate specificity and activity of caspases is described. Furthermore, the evolution of immobilization from the solid support used in peptide synthesis to nanocarriers is presented. Taken together, the examples presented here demonstrate immobilized peptides as a multifunctional tool, which can be successfully used to solve multiple analytical problems.

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Section: Discussion: Peptide Biosensors-advantages and Applicationsmentioning

confidence: 99%

Section: Discussion: Peptide Biosensors-advantages and Applicationsmentioning

confidence: 99%

Section: Capturing Carbonylated Compoundsmentioning

confidence: 99%

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Veni, Vidi, Vici: Immobilized Peptide-Based Conjugates as Tools for Capture, Analysis, and Transformation

et al. 2022

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“…In the second approach, we used the hydroxylamine derivative attached to the polymer, recently developed by our group for the enrichment of samples in carbonylated peptides and other compounds with reactive carbonyl groups, to confirm the presence of a deamination product. The mixture of compounds obtained after the reaction of peptides (H-AFAK-NH 2 or H-RAKAFKA-NH 2 ) with lactose was reacted with hydroxylamine immobilized on resin according to the protocol placed in Section .…”

Section: Results and Discussionmentioning

confidence: 99%

“…In the second approach, we used the hydroxylamine derivative attached to the polymer, recently developed by our group 26 for the enrichment of samples in carbonylated peptides and other compounds with reactive carbonyl groups, to confirm the presence of a deamination product. The mixture of compounds obtained after the reaction of peptides (H- O and H 2 16 O in the presence of NaBH 4 (A); ESI-MS spectrum for a retention time of 6.9 min with the zoom isotopic pattern for investigated compounds, identified as reduced α-hydroxyacyl (B) (the whole spectrum with identification of all signals is placed in the Supporting Information).…”

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High-Temperature, Solid-Phase Reaction of α-Amino Groups in Peptides with Lactose and Glucose: An Alternative Mechanism Leading to an α-Ketoacyl Derivative

Kijewska

Zawadzka

Stefanowicz

2023

J. Agric. Food Chem.

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The reaction of proteins with reducing sugars results in the formation of Amadori products, which involves the Nterminal group and/or ε-amino group of the lysine side chain. However, less attention has been given to the reactivity of the Nterminus of a peptide chain under similar conditions. In our work, we focused on the reaction of the α-amino group of peptides in the presence of a reducing sugar, specifically lactose. We optimized the reaction conditions of model peptides with lactose in the solid phase and showed that temperatures above 120 °C lead to the deamination of the N-terminal amino acid moiety, ultimately resulting in α-ketoacids. We carried out detailed studies to confirm the structure of the deaminated product using analytical methods such as ESI-MS and LC−MS/MS, as well as chemical methods that involved the reduction of the carbonyl group combined with isotopic exchange and the reactivity of the carbonyl group with the hydroxylamine derivative. The structure of the reaction product was also confirmed by chemical synthesis. We suggested plausible mechanisms for the formation of the deaminated product and considered the probable path of its formation. Our aim was to determine whether the reaction proceeds according to the Streckerbased mechanism and direct imine isomerization by carrying out reactions of model peptides in the presence of lactose under aerobic and anaerobic conditions and comparing the results obtained. KEYWORDS: LC−MS/MS analysis, lactosylated peptides, α-ketoacid derivatives, deamination catalyzed by a reducing sugar ■ HIGHLIGHTS• LC−MS/MS analysis of lactosylated peptides.• Deamination of the N-terminal amino acid by a reducing sugar. • Chemoselective reaction of the hydroxylamine derivative with the deamination product.

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A Bacterial Cytochrome P450 Enzyme Catalyzes Multistep Oxidation Reactions in Pyrroindomycin Biosynthesis

Wang

Chen

et al. 2023

Chin. J. Chem.

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Comprehensive SummaryCytochrome P450 enzymes (P450s) belong to a large family of oxidative hemeproteins and catalyze highly diverse oxygenation reactions that are involved in the biosynthesis of various natural products. Here, we report a multifunctional cytochrome P450 enzyme, PyrE2, which catalyzes the regioselective, successive 6‐electron oxidation of an inert methyl group to produce a carboxyl product through formation of the hydroxyl and aldehyde intermediates in pyrroindomycin biosynthesis. The time‐course biotransformation was characterized by the presence of the hydroxyl and aldehyde intermediates, the lag of the formation of the carboxyl product, and the subsequent loss of both intermediates, indicating that each 2‐electron oxidation exhibits the distributive mechanism that requires substrate binding and product releasing. Bioinformatics analysis shows that the homologs of pyrE2 are common in the gene clusters of the spirotetronates varying in the oxidative state of the corresponding exocyclic carbon, indicating the generality and diversity of P450‐catalyzed oxygenation in related biosynthetic pathways.

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Selective ESI-MS detection of carbonyl containing compounds by aminooxyacetic acid immobilized on a resin

Cited by 3 publications

References 49 publications

Veni, Vidi, Vici: Immobilized Peptide-Based Conjugates as Tools for Capture, Analysis, and Transformation

Veni, Vidi, Vici: Immobilized Peptide-Based Conjugates as Tools for Capture, Analysis, and Transformation

High-Temperature, Solid-Phase Reaction of α-Amino Groups in Peptides with Lactose and Glucose: An Alternative Mechanism Leading to an α-Ketoacyl Derivative

A Bacterial Cytochrome P450 Enzyme Catalyzes Multistep Oxidation Reactions in Pyrroindomycin Biosynthesis

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