Ditryptophan Cross-Links as Novel Products of Protein Oxidation

AUTOR(ES)

Paviani, Verônica, Galdino, Gabriel T., Prazeres, Janaina N. dos, Queiroz, Raphael F., Augusto, Ohara

FONTE

J. Braz. Chem. Soc.

DATA DE PUBLICAÇÃO

2018-05

RESUMO

Protein oxidation is an unavoidable consequence of aerobic metabolism. The oxidation of most proteins residues is non-repairable and may affect protein structure and function. In particular, protein cross-links arising from oxidative modifications are presumably toxic to cells because they may accumulate and induce protein aggregation. However, most of these irreversible protein cross-links remain partially characterized. Up to very recently, ditryptophan cross-links (Trp-Trp), in particular, have been largely disregarded in the literature. Here, we briefly review studies showing that Trp-Trp cross-links can be formed in proteins exposed to a variety of oxidants. The challenges to fully characterize Trp-Trp cross-links are discussed as well as their potential roles in protein dysfunction and aggregation.

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