By Jing Yu
Water and moisture undermine powerful adhesion to polar surfaces. Marine mussels, even though, in achieving sturdy underwater adhesion utilizing a set of proteins which are odd in having excessive degrees of three, 4-dihydroxyphenylalanine (Dopa). Mussel adhesion has encouraged a variety of reports on constructing the following iteration of rainy adhesives. This thesis offers fresh development in figuring out the fundamental floor and intermolecular interactions hired by way of mussels to accomplish powerful and sturdy rainy adhesion. the skin forces equipment (SFA) and numerous different strategies 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 a number of mussel adhesive proteins. the implications during this thesis convey that Dopa performs a vital position in mussel adhesion and that mussels delicately regulate the interfacial redox atmosphere to accomplish powerful and sturdy Dopa mediated adhesion. The interaction among Dopa and hydrophobic interactions can be obtrusive in mussel adhesion.
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Additional info for Adhesive Interactions of Mussel Foot Proteins
When water molecules interact with nonpolar molecules (such as hydrocarbons) that are incapable of forming hydrogen bonds with water molecules, they lose the ability of maintaining their normal H-bonding network. Water solves this problem by two ways, which give the two limits of the hydrophobic interactions. When the nonpolar solute molecule is small (the diameter is typically smaller than 1 nm), water molecules can rearrange themselves around it without breaking their H-bonding network. Although its rearrangement requires an entropy penalty, it is energetically favorable .
A–e) Mfp-3 variants are secreted into the distal depression (a) and partially adsorbed by Dopa-mediated H-bonds to the mica surface. The oxidation of unadsorbed Dopa to dopaquinone (b) is counteracted by reducing thiolates (c) in Mfp-6, which enables enhanced adsorption (d). Depletion of thiolate pairs in Mfp-6 transforms Mfp-6 into a cross-linker with Mfp-3 (e). Red reduced, ox oxidized of the polysiloxane surface of mica  probably shields Dopa H-bonded to mica from oxidation (Fig. 6b). As predicted by Bell theory and by analogy to the A-T pairs in DNA, the well-oriented bidentate hydrogen bonding (E = ~ −28kT) of Dopa to mica should have a binding lifetime (τ = τ0e− E/kT) that is 106 times as long as the monodentate form (E = ~ −14kT) .
A) Mfp-3 on mica at pH 3. (b) A 30 % loss of adhesion was measured after adding 400 pmol NaIO4 into the gap at pH 3. (c) Near-abolition of adhesion after adding 600 pmol NaIO4 into the gap solution at pH 3. 25 mM) into the gap solution recovered about 30 % of the adhesion Clearly, Dopa in purified Mfp-3 is susceptible to oxidation during testing in the SFA. In contrast, however, biochemical analysis of plaques shows that the Dopa content of adhesive proteins such as Mfp-3 and Mfp-5 remains largely intact while they reside in the plaque footprints .