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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Electrospray ionization mass spectrometry applied to study the radical acetylation of amino acids, peptides and proteins

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Author(s):
Alves, Atecla N. L. [1] ; Jedlicka, Leticia D. L. [2] ; Massari, Julio [3] ; Juliano, Maria A. [4] ; Bechara, Etelvino J. H. [1, 3] ; Assuncao, Nilson A. [1, 2]
Total Authors: 6
Affiliation:
[1] Univ Fed Sao Paulo, Inst Ciencias Ambientais Quim & Farmaceut, BR-09972270 Diadema, SP - Brazil
[2] Univ Fed Sao Paulo, Escola Paulista Med, BR-04023062 Sao Paulo - Brazil
[3] Univ Sao Paulo, Inst Quim, BR-05513890 Sao Paulo - Brazil
[4] Univ Fed Sao Paulo, Dept Bioquim, BR-04044020 Sao Paulo - Brazil
Total Affiliations: 4
Document type: Journal article
Source: Journal of the Brazilian Chemical Society; v. 24, n. 12, p. 1983+, DEC 2013.
Web of Science Citations: 4
Abstract

Recently, our group proposed a process that generated acetyl radicals in a reaction medium buffered with a diacetyl/peroxynitrite system. Diacetyl is a flavoring agent in food, cigarettes and drinks. Peroxynitrite is found in mitochondria, and in certain conditions, such as an infection in humans, its concentration is augmented significantly. In biological systems, radical compounds can easily modify the structure and activity of nucleic acids, proteins and other biomolecules, causing significant oxidative stress. Based on paramagnetic resonance and mass spectrometry data, this work discusses products that prove acetyl radicals are produced and are able to form stable covalent bonds with amino acid (acetylated products), peptide and protein adducts. These materials were separated and detected by capillary electrophoresis coupled with tandem mass spectrometry or offline mass spectrometry. The reaction medium contained a 1:2 mixture of diacetyl and peroxynitrite dissolved in 200 mmol L-1 of pH 7.2 sodium phosphate buffer. These experiments also reveal the double acetylation of lysine, demonstrating the high reactivity of these compounds when in contact with nitrogen-containing biomolecules readily found in biological systems. These structural changes might be an epigenetic source of post-translational protein modification. (AU)

FAPESP's process: 12/02514-9 - Use of proteomics techniques to study radical acetylation of proteins triggered by products of the reaction biacetyl/peroxinitrite
Grantee:Nilson Antonio de Assunção
Support Opportunities: Regular Research Grants