| Texto completo | |
| Autor(es): |
Paviani, Veronica
[1]
;
Galdino, Gabriel T.
[1]
;
dos Prazeres, Janaina N.
[1]
;
Queiroz, Raphael F.
[2]
;
Augusto, Ohara
[1]
Número total de Autores: 5
|
| Afiliação do(s) autor(es): | [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
Número total de Afiliações: 2
|
| Tipo de documento: | Artigo Científico |
| Fonte: | Journal of the Brazilian Chemical Society; v. 29, n. 5, p. 925-933, MAY 2018. |
| Citações Web of Science: | 3 |
| 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. (AU) | |
| Processo FAPESP: | 13/07937-8 - Redoxoma |
| Beneficiário: | Ohara Augusto |
| Modalidade de apoio: | Auxílio à Pesquisa - Centros de Pesquisa, Inovação e Difusão - CEPIDs |