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Phase-dependent redox insulation in mussel adhesion.

ABSTRACT: Catecholic 3,4-dihydroxyphenyl-l-alanine (Dopa) residues in mussel foot proteins (mfps) contribute critically to mussel (Mytilus californianus) plaque adhesion, but only if protected from oxidation at the adhesive-substratum interface. Dopa oxidation is thermodynamically favorable in seawater yet barely detectable in plaques; therefore, we investigated how plaques insulate Dopa-containing mfps against oxidation. Seawater sulfate triggers an mfp3 and mfp6 liquid-liquid phase separation (LLPS). By combining plaque cyclic voltammetry with electrophoresis, mass spectrometry, and redox-exchange chemistry, we show that Dopa-containing mfp3 and mfp6 in phase-separated droplets remain stable despite rapid oxidation in the surrounding equilibrium solution. The results suggest that a cohort of oxidation-prone proteins is endowed with phase-dependent redox stability. Moreover, in forming LLPS compartments, Dopa proteins become reservoirs of chemical energy.

SUBMITTER: Valois E

PROVIDER: S-EPMC7269650 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature

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Phase-dependent redox insulation in mussel adhesion.

Valois Eric E Mirshafian Razieh R Waite J Herbert JH

Science advances 20200603 23

Catecholic 3,4-dihydroxyphenyl-l-alanine (Dopa) residues in mussel foot proteins (mfps) contribute critically to mussel (<i>Mytilus californianus</i>) plaque adhesion, but only if protected from oxidation at the adhesive-substratum interface. Dopa oxidation is thermodynamically favorable in seawater yet barely detectable in plaques; therefore, we investigated how plaques insulate Dopa-containing mfps against oxidation. Seawater sulfate triggers an mfp3 and mfp6 liquid-liquid phase separation (LL ...[more]

PMID: 32537498

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