at Google ScholarTitle data
Wang, Jia ; Suhre, Michael H. ; Scheibel, Thomas:
A mussel polyphenol oxidase-like protein shows thiol-mediated antioxidantactivity.
In: European Polymer Journal.
Vol. 113
(2019)
.
- pp. 305-312.
ISSN 1873-1945
DOI: https://doi.org/10.1016/j.eurpolymj.2019.01.069
Abstract in another language
Marine mussels adhere underwater to a variety of substrates using adhesive proteins with post-translationallymodified amino acids, such as 3,4-dihydroxyphenylalanine (DOPA) residues, as a key chemical signature. DOPAcan auto-oxidize easily in seawater reducing the adhesion strength, but contributing to subsequent cohesion(cross-linking) of the underlying proteins. To maintain both reduced and oxidized forms of DOPA with corre-sponding adhesion and cohesion properties, strict redox regulation is necessary for mussel underwater adhesion.In this study, a full-length polyphenol oxidase-like protein (PPOL) fromMytilusgalloprovincialiswas identifiedafter screening of a mussel foot cDNA library using different degenerated PCR primers. The recombinant PPOL(rPPOL) was successfully produced inEscherichiacoli. The rPPOL exhibits thiol-dependent antioxidant activitysuppressing DOPA oxidation. This finding provides insights into how DOPA chemistry could be regulated andpresumably inspires future applications of DOPA-mediated adhesion materials.