Ditryptophan Cross-Links as Novel Products of Protein Oxidation

Author(s)

Paviani, Veronica ^[1] ; Galdino, Gabriel T. ^[1] ; dos Prazeres, Janaina N. ^[1] ; Queiroz, Raphael F. ^[2] ; Augusto, Ohara ^[1]

Affiliation

^[1] Univ Sao Paulo, Inst Quim, Dept Bioquim, Ave Lineu Prestes 748, BR-05508000 Sao Paulo, SP - Brazil

^[2] Univ Estadual Sudoeste Bahia, Dept Ciencias Nat, BR-45083900 Vitoria Da Conquista, BA - Brazil

• Document type: Journal article
• Source: Journal of the Brazilian Chemical Society; v. 29, n. 5, p. 925-933, MAY 2018.
• Web of Science Citations: 3

Abstract

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. (AU)

• FAPESP's process: 13/07937-8 - Redoxome - Redox Processes in Biomedicine
• Grantee: Ohara Augusto
• Support Opportunities: Research Grants - Research, Innovation and Dissemination Centers - RIDC