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Mussel protein adhesion depends on interprotein thiol-mediated redox modulation

Nature Chemical Biology volume 7, pages 588–590 (2011)Cite this article

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Abstract

Mussel adhesion is mediated by foot proteins (mfps) rich in a catecholic amino acid, 3,4-dihydroxyphenylalanine (dopa), capable of forming strong bidentate interactions with a variety of surfaces. A tendency toward facile auto-oxidation, however, often renders dopa unreliable for adhesion. We demonstrate that mussels limit dopa oxidation during adhesive plaque formation by imposing an acidic, reducing regime based on the thiol-rich mfp-6, which restores dopa by coupling the oxidation of thiols to dopaquinone reduction.

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Figure 1: Byssal adhesion in the California mussel Mytilus californianus.
Figure 2: Adhesion of mfp-3 at different pH before and after mfp-6 addition.
Figure 3: Redox control and the stepwise adsorption and cross-linking of mfp-3.

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Acknowledgements

We thank the US National Institutes of Health (R01 DE018468), the National Science Foundation Materials Science & Engineering Research Center Program (DM R05-20415) and the Human Frontiers of Science Program for supporting this research. C. Thorpe provided helpful insights about thiol chemistry. S. Nicklisch and P. Schmitt introduced us to the DPPH assay.

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Author notes

  1. Jing Yu and Wei Wei: These authors contributed equally to this work.

Authors and Affiliations

  1. Department of Chemical Engineering, University of California, Santa Barbara, Santa Barbara, California, USA.,

    Jing Yu & Jacob N Israelachvili

  2. Materials Research Laboratory, University of California, Santa Barbara, Santa Barbara, California, USA.,

    Wei Wei

  3. Department of Molecular, Cell & Developmental Biology, University of California, Santa Barbara, Santa Barbara, California, USA.,

    Eric Danner, Rebekah K Ashley & J Herbert Waite

Authors
  1. Jing Yu
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  2. Wei Wei
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  5. Jacob N Israelachvili
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  6. J Herbert Waite
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Contributions

J.Y. designed and performed the SFA experiments; W.W. purified and modified proteins; E.D. and R.K.A. contributed protein; J.H.W. wrote the manuscript and designed and co-supervised the whole project with J.N.I., who helped analyze the results.

Corresponding authors

Correspondence to Jacob N Israelachvili or J Herbert Waite.

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The authors declare no competing financial interests.

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Yu, J., Wei, W., Danner, E. et al. Mussel protein adhesion depends on interprotein thiol-mediated redox modulation. Nat Chem Biol 7, 588–590 (2011). https://doi.org/10.1038/nchembio.630

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