Titlebook: Adhesive Interactions of Mussel Foot Proteins; Jing Yu Book 2014 Springer International Publishing Switzerland 2014 Mfps.Mica.Mussel Foot

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https://doi.org/10.1007/978-3-642-85723-2s a side chain, dopa is capable of strong bidentate interactions with a variety of surfaces, but its susceptibility to oxidation often renders it unreliable for adhesion. Mussels limit Dopa oxidation by imposing an acidic, reducing regime in the confined space of Mfp deposition. Using the surface fo

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Grundbegriffe zum Baumanagement,synthetic polymer systems. However, Dopa is notoriously susceptible to oxidation, and this represents a major challenge for the practical translation of mussel adhesion. Using a surface forces apparatus to investigate the adhesion of Mfp-3 (mussel foot protein-3) ., a protein variant of the Mfp-3 fa

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Grundbegriffe zum Baumanagement,esives and coatings. Although the role of Dopa on mussel adhesion has been carefully studied, a full picture of the whole binding mechanism of mussel proteins is still unclear due to the complexity of the protein molecules and molecular processes involved. We designed three short peptides based on m

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Adhesive Interactions of Mussel Foot Proteins978-3-319-06031-6Series ISSN 2190-5053 Series E-ISSN 2190-5061

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Book 2014 that are peculiar in having high levels of 3, 4-dihydroxyphenylalanine (Dopa). Mussel adhesion has inspired numerous studies on developing the next generation of wet adhesives. This thesis presents recent progress in understanding the basic surface and intermolecular interactions employed by mussel

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https://doi.org/10.1007/978-3-642-85723-2. The SFA results show that the adhesion properties of Mfp-3 are closely coupled to the redox state of Dopa. The oxidation of Dopa to Dopaquinone diminishes the adhesion of Mfp-3 on mica surfaces. Dopaquinone tautomers could be associated with structural changes in oxidized adhesive mussel foot proteins such as Mfp-3.

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https://doi.org/10.1007/978-3-642-85723-2 restores Mfp-3 adhesion by coupling the oxidation of thiols to the reduction of Dopaquinones. How mussels preserve adhesive Dopa-containing proteins from oxidation has considerable biological and technological value.

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Book 2014ns. The results in this thesis show that Dopa plays an essential role in mussel adhesion and that mussels delicately control the interfacial redox environment to achieve strong and durable Dopa mediated adhesion. The interplay between Dopa and hydrophobic interactions is also evident in mussel adhesion.