Mussel protein adhesion depends on thiol-mediated redox modulation

Mussel adhesion is mediated by foot proteins (mfp) rich in a catecholic amino acid, 3, 4-dihydroxyphenylalanine (dopa), capable of forming strong bidentate interactions with a variety of surfaces. A facile tendency toward auto-oxidation, however, often renders dopa unreliable for adhesion. Mussels l...

Descripción completa

Detalles Bibliográficos
Autores principales: Yu, Jing, Wei, Wei, Danner, Eric, Ashley, Rebekah K., Israelachvili, Jacob N., Waite, J. Herbert
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2011
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3158268/
https://www.ncbi.nlm.nih.gov/pubmed/21804534
http://dx.doi.org/10.1038/nchembio.630
Descripción
Sumario:Mussel adhesion is mediated by foot proteins (mfp) rich in a catecholic amino acid, 3, 4-dihydroxyphenylalanine (dopa), capable of forming strong bidentate interactions with a variety of surfaces. A facile tendency toward auto-oxidation, however, often renders dopa unreliable for adhesion. Mussels limit dopa oxidation during adhesive plaque formation by imposing an acidic, reducing regime based on thiol-rich mfp-6, which restores dopa by coupling the oxidation of thiols to dopaquinone reduction.

Ejemplares similares