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      Mussel protein adhesion depends on thiol-mediated redox modulation

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          Abstract

          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.

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          Understanding Marine Mussel Adhesion

          Heather Silverman, Francisco Roberto (2007)
          In addition to identifying the proteins that have a role in underwater adhesion by marine mussels, research efforts have focused on identifying the genes responsible for the adhesive proteins, environmental factors that may influence protein production, and strategies for producing natural adhesives similar to the native mussel adhesive proteins. The production-scale availability of recombinant mussel adhesive proteins will enable researchers to formulate adhesives that are water-impervious and ecologically safe and can bind materials ranging from glass, plastics, metals, and wood to materials, such as bone or teeth, biological organisms, and other chemicals or molecules. Unfortunately, as of yet scientists have been unable to duplicate the processes that marine mussels use to create adhesive structures. This study provides a background on adhesive proteins identified in the blue mussel, Mytilus edulis, and introduces our research interests and discusses the future for continued research related to mussel adhesion.
          Article 0 comments Cited 125 times – based on 0 reviews     Review now
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            Adhesion mechanisms of the mussel foot proteins mfp-1 and mfp-3.

            Qi Lin, Delphine Gourdon, Chengjun Sun … (2007)
            Mussels adhere to a variety of surfaces by depositing a highly specific ensemble of 3,4-dihydroxyphenyl-l-alanine (DOPA) containing proteins. The adhesive properties of Mytilus edulis foot proteins mfp-1 and mfp-3 were directly measured at the nano-scale by using a surface forces apparatus (SFA). An adhesion energy of order W approximately 3 x 10(-4) J/m(2) was achieved when separating two smooth and chemically inert surfaces of mica (a common alumino-silicate clay mineral) bridged or "glued" by mfp-3. This energy corresponds to an approximate force per plaque of approximately 100 gm, more than enough to hold a mussel in place if no peeling occurs. In contrast, no adhesion was detected between mica surfaces bridged by mfp-1. AFM imaging and SFA experiments showed that mfp-1 can adhere well to one mica surface, but is unable to then link to another (unless sheared), even after prolonged contact time or increased load (pressure). Although mechanistic explanations for the different behaviors are not yet possible, the results are consistent with the apparent function of the proteins, i.e., mfp-1 is disposed as a "protective" coating, and mfp-3 as the adhesive or "glue" that binds mussels to surfaces. The results suggest that the adhesion on mica is due to weak physical interactions rather than chemical bonding, and that the strong adhesion forces of plaques arise as a consequence of their geometry (e.g., their inability to be peeled off) rather than a high intrinsic surface or adhesion energy, W.
            Article 0 comments Cited 103 times – based on 0 reviews     Review now
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              Strong reversible Fe3+-mediated bridging between dopa-containing protein films in water.

              Hongbo Zeng, Dong Soo Hwang, Jacob Israelachvili … (2010)
              Metal-containing polymer networks are widespread in biology, particularly for load-bearing exoskeletal biomaterials. Mytilus byssal cuticle is an especially interesting case containing moderate levels of Fe(3+) and cuticle protein-mussel foot protein-1 (mfp-1), which has a peculiar combination of high hardness and high extensibility. Mfp-1, containing 13 mol % of dopa (3, 4-dihydroxyphenylalanine) side-chains, is highly positively charged polyelectrolyte (pI approximately 10) and didn't show any cohesive tendencies in previous surface forces apparatus (SFA) studies. Here, we show that Fe(3+) ions can mediate unusually strong interactions between the positively charged proteins. Using an SFA, Fe(3+) was observed to impart robust bridging (W(ad) approximately 4.3 mJ/m(2)) between two noninteracting mfp-1 films in aqueous buffer approaching the ionic strength of seawater. The Fe(3+) bridging between the mfp-1-coated surfaces is fully reversible in water, increasing with contact time and iron concentration up to 10 microM; at 100 microM, Fe(3+) bridging adhesion is abolished. Bridging is apparently due to the formation of multivalent dopa-iron complexes. Similar Fe-mediated bridging (W(ad) approximately 5.7 mJ/m(2)) by a smaller recombinant dopa-containing analogue indicates that bridging is largely independent of molecular weight and posttranslational modifications other than dopa. The results suggest that dopa-metal interactions may provide an energetic new paradigm for engineering strong, self-healing interactions between polymers under water.
              Article 0 comments Cited 101 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (nlm-journal-id): 101231976
                Journal ID (pubmed-jr-id): 32624
                Journal ID (nlm-ta): Nat Chem Biol
                Title: Nature chemical biology
                ISSN (Print): 1552-4450
                ISSN (Electronic): 1552-4469
                Publication date Nihms-submitted: 9 June 2011
                Publication date (Electronic): 31 July 2011
                Publication date PMC-release: 1 March 2012
                Volume: 7
                Issue: 9
                Pages: 588-590
                Affiliations
                [1 ] Department of Chemical Engineering, University of California, Santa Barbara, CA 93106
                [2 ] Materials Research Laboratory, University of California, Santa Barbara, CA 93106
                [3 ] Department of Molecular, Cell & Developmental Biology, University of California, Santa Barbara, CA 93106
                Author notes
                [*]

                authors contributed equally

                Article
                Manuscript ID: nihpa301942
                DOI: 10.1038/nchembio.630
                PMC ID: 3158268
                PubMed ID: 21804534
                SO-VID: 6d6d7dab-34e6-4225-a506-5b4e916d9fd3
                License:

                Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms

                History
                Funding
                Funded by: National Institute of Dental and Craniofacial Research : NIDCR
                Award ID: R01 DE018468-04 || DE
                Funded by: National Institute of Dental and Craniofacial Research : NIDCR
                Award ID: R01 DE018468-03 || DE
                Funded by: National Institute of Dental and Craniofacial Research : NIDCR
                Award ID: R01 DE018468-02 || DE
                Funded by: National Institute of Dental and Craniofacial Research : NIDCR
                Award ID: R01 DE018468-01A1 || DE
                Categories
                Subject: Article

                ScienceOpen disciplines: Biochemistry
                Data availability:
                ScienceOpen disciplines: Biochemistry

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