Adhesive Interactions of Mussel Foot Proteins by Jing Yu

By Jing Yu

Water and moisture undermine powerful adhesion to polar surfaces. Marine mussels, even if, in achieving sturdy underwater adhesion utilizing a set of proteins which are atypical in having excessive degrees of three, 4-dihydroxyphenylalanine (Dopa). Mussel adhesion has encouraged quite a few reports on constructing the subsequent new release of rainy adhesives. This thesis offers fresh growth in figuring out the fundamental floor and intermolecular interactions hired by means of mussels to accomplish robust and sturdy rainy adhesion. the outside forces gear (SFA) and numerous different suggestions have been utilized to degree the interactions among mussel foot protein-3 fast (Mfp-3 fast) and the version substrate, mica, in addition to the interactions among quite a few mussel adhesive proteins. the implications during this thesis exhibit that Dopa performs an important function in mussel adhesion and that mussels delicately keep watch over the interfacial redox atmosphere to accomplish robust and sturdy Dopa mediated adhesion. The interaction among Dopa and hydrophobic interactions can be obvious in mussel adhesion.

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Apparently, during contact, Mfp-3 chains already bound to a mica surface rearrange to span the gap to bind another surface. A single Mfp-3 film had a thickness (hard wall) of 5 nm when compressed. The strong adhesion between two Mfp-3 films at pH 3 (Fig. 15, n = 6) within a few minutes of raising the pH. 5, only weak adhesion remained. Given that the autoxidation of catechols increases with increasing pH [19], I tested whether adhesion loss is correlated with Dopa oxidation. Titration with an oxidant at pH 3 supports this premise (Fig.

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