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- W4220787629 abstract "3,4-Dihydroxyphenylalanine (Dopa) is a versatile molecule that enables marine mussels to achieve successful underwater adhesion. However, due to its complicated redox chemistry and vulnerability to oxidation, controlling surface adhesion and cohesion has been a challenging issue to overcome. Foot protein type 6 (fp-6), a thiol-rich interfacial mussel adhesive protein, has been reported as a proteinaceous antioxidant for mussels that helps Dopa maintain surface adhesion ability. In this study, we focused on the role of fp-6 in oxidized Dopa. The effect on the tautomer equilibrium of oxidized Dopa was investigated using recombinant fp-6 (rfp-6) and Dopa-incorporated foot protein type 3 fast variant (drfp-3F), which were produced in bacterial cells. The redox chemistry of Dopa in drfp-3F and the role of rfp-6 were observed using a UV-vis spectrophotometer and a surface forces apparatus (SFA). We discovered that rfp-6 shifts the tautomer equilibrium to ΔDopa as a preferred tautomer for oxidized Dopa in drfp-3F and makes drfp-3F better on underwater surface adhesion." @default.
- W4220787629 created "2022-04-03" @default.
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- W4220787629 date "2022-03-08" @default.
- W4220787629 modified "2023-09-24" @default.
- W4220787629 title "Thiol-Rich fp-6 Controls the Tautomer Equilibrium of Oxidized Dopa in Interfacial Mussel Foot Proteins" @default.
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- W4220787629 doi "https://doi.org/10.1021/acs.langmuir.1c03239" @default.
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