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Design of New Probes for Oxidized Amino Acids Localization

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Design of New Probes for Oxidized Amino Acids

Localization

Mathieu Esgulian, Luc Camoin, Mathieu Cassien, Yves Toiron, Sylvia Pietri,

Sophie Thétiot-Laurent

To cite this version:

Mathieu Esgulian, Luc Camoin, Mathieu Cassien, Yves Toiron, Sylvia Pietri, et al.. Design of New

Probes for Oxidized Amino Acids Localization. Proceedings, MDPI, 2019, 22 (1), pp.39.

�10.3390/pro-ceedings2019022039�. �hal-02393325�

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Proceedings 2019, 22, 39; doi:10.3390/proceedings2019022039 www.mdpi.com/journal/proceedings

Abstract

Design of New Probes for Oxidized Amino Acids

Localization

Mathieu Esgulian

1,

*, Luc Camoin

2

, Mathieu Cassien

1

, Yves Toiron

2

, Sylvia Pietri

1

and

Sophie Thétiot-Laurent

1,

*

1 Aix Marseille Université, CNRS UMR 7273, Institue de Chimie Radicalaire, Equipe Sonde Moléculaires en Biologie et Stress Oxydant, 13013 Marseille, France

2 CRCM, Inserm, 13009 Marseille, France

* Correspondence: mathieu.esgulian@univ-amu.fr (M.E.); sophie.thetiot-laurent@univ-amu.fr (S.T.-L.)

† Presented at the 2nd Molecules Medicinal Chemistry Symposium (MMCS): Facing Novel Challenges in Drug Discovery, Barcelona, Spain, 15–17 May 2019.

Published: 8 August 2019

Keywords: protein carbonyls; probes; hydrazine; click chemistry

Protein carbonyls (PC) are oxidative damage observed in many diseases. Proteins are possibly the

most immediate vehicle for inflicting oxidative damage on cells because they are often catalysts [1]. A

fluorometric and UV-absorption method have been developed to quantify PC in blood and tissues

samples by labeling with two hydrazines: 7-hydrazino-4-nitrobenzo-2,1,3-oxadiazole (NBDH) and

dinitrophenylhydrazine (DNPH), respectively [2,3]. These methods are based on the selective hydrazone

formation between the carbonyls group of oxidized protein to yield a strong fluorescent/UV-absorption

adduct that is then quantified.

Here, we will describe our study on NBDH’s and DNPH’s derivatives to generate new PC-probes

bearing an alkyne moiety. In a first step, the hydrazine moiety reacted specifically with protein

carbonyls and in a second step, a click reaction was performed between the alkyne moiety and a

cleavable resin [4] to yield a PC’s enrichment. Theses probes have been explored on oxidized bovine

serum albumin (OxBSA) for PC-labeling, and the possible sites of oxidation of isolated labelled PC

will be studied by LC-MS and proteomics experiments.

References

1. Dalle-Donne, I.; Rossi, R.; Giustarini, D.; Milzani, A.; Colombo, R. Protein carbonyl groups as biomarkers of oxidative stress. Clin. Chim. Acta 2003, 329, 23–38.

2. Stocker, P.; Ricquebourg, E.; Vidal, N.; Villard, C.; Lafitte, D.; Sellami, L.; Pietri, S. Fluorimetric screening assay for protein carbonyl evaluation in biological samples. Anal. Biochem. 2015, 482, 55–61.

3. Vidal, N.; Cavaille, J.P.; Graziani, F.; Robin, M.; Ouari, O.; Stocker, P. High throughput assay for

evaluation of reactive carbonyl scavenging capacity. Redox Biology 2014, 2, 590–598.

4. Sibbersen, C.; Lykke, L.; Gregersen, N.; Jørgensen, K.A.; Johannsen, M. A cleavable azide resin for direct click chemistry mediated enrichment of alkyne-labeled proteins. Chem. Commun. 2014, 50, 12098–12100.

© 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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