Download e-book for kindle: Adhesive Interactions of Mussel Foot Proteins by Jing Yu

By Jing Yu

ISBN-10: 3319060309

ISBN-13: 9783319060309

ISBN-10: 3319060317

ISBN-13: 9783319060316

Water and moisture undermine powerful adhesion to polar surfaces. Marine mussels, although, in attaining sturdy underwater adhesion utilizing a collection of proteins which are unusual in having excessive degrees of three, 4-dihydroxyphenylalanine (Dopa). Mussel adhesion has encouraged a variety of reviews on constructing the subsequent iteration of rainy adhesives. This thesis provides fresh growth in knowing the elemental floor and intermolecular interactions hired by way of mussels to accomplish robust and sturdy rainy adhesion. the outside forces gear (SFA) and numerous different innovations 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 variety of mussel adhesive proteins. the consequences during this thesis exhibit that Dopa performs an important position in mussel adhesion and that mussels delicately regulate the interfacial redox surroundings to accomplish powerful and sturdy Dopa mediated adhesion. The interaction among Dopa and hydrophobic interactions is additionally obvious in mussel adhesion.

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Sample text

8) A similar equation can be derived for separating two dissimilar media 1 and 2 in medium 3: W132 = γ 13 + γ 23 − γ 12 . 2 Adhesion Energies and Adhesion Forces Although sometimes used interchangeably, we have to notice that the adhesion energy and the adhesion force are two different things. Strictly, the adhesion energy is an equilibrium term, and it should only depend on the initial and final states. To measure it accurately, the measurement has to be infinitely slow or, in other words, in a reversible process.

In the 1970s to measure the VDW forces in air down to a few nanometers [14]. Since then, the SFA technique has been continuously modified [15, 16]. The ability to measure forces in various liquids greatly extended the territory of the SFA, allowing it to measure almost all the surface forces: the VDW, electrostatic, DLVO, hydrophobic, hydration, and polymer-­ mediated steric forces [5, 14–16]. Starting in the 1990s, the SFA technique has been applied to measure the interactions in complex biological systems involving ­membranes and membrane proteins [17–19].

5 differed by an order of magnitude in two reports [3, 13]. The holdfast or byssus of a California mussel (Mytilus californianus Conrad) resembles a bundle of threads, each of which is distally tipped with a flared adhesive plaque (Fig. 1a). About ten plaque proteins have been characterized and half of these are unique to the plaque whereas the others are distributed in both threads and plaques [14]. The mussel assembles each new plaque in a few minutes from proteins stockpiled in its foot. The first proteins the foot squirts onto the surface of a rock are mussel foot proteins Mfp-3 and Mfp-5 with Dopa contents of 20 mol% and 30 mol%, respectively [1, 2] (Fig.

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Adhesive Interactions of Mussel Foot Proteins by Jing Yu


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