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Nanomechanics of Cation–π Interactions in Aqueous Solution
Lu, Qingye,Oh, Dongyeop X.,Lee, Youngjin,Jho, Yongseok,Hwang, Dong Soo,Zeng, Hongbo WILEY‐VCH Verlag 2013 Angewandte Chemie Vol.125 No.14
<P><B>Eine erste direkte Untersuchung</B> der Nanomechanik von Kation‐π‐Wechselwirkungen in wässrigem Medium wurde mit einem Oberflächenkraftmessgerät durchgeführt und durch theoretische Simulationen ergänzt. Das Tetraethylammonium‐Ion (TEA) verhindert die Adhäsion von Polytryptophan (PTrp) und Poly‐<SMALL>L</SMALL>‐lysin (PLL) mit einer 100‐fach höheren Empfindlichkeit als das K<SUP>+</SUP>‐Ion (PS=Polystyrol, PTyr=Poly‐<SMALL>L</SMALL>‐tyrosin, ACh=Acetylcholin).</P>
Adhesion of mussel foot proteins to different substrate surfaces
Lu, Qingye,Danner, Eric,Waite, J. Herbert,Israelachvili, Jacob N.,Zeng, Hongbo,Hwang, Dong Soo The Royal Society 2013 Journal of the Royal Society, Interface Vol.10 No.79
<P> Mussel foot proteins (mfps) have been investigated as a source of inspiration for the design of underwater coatings and adhesives. Recent analysis of various mfps by a surface forces apparatus (SFA) revealed that mfp-1 functions as a coating, whereas mfp-3 and mfp-5 resemble adhesive primers on mica surfaces. To further refine and elaborate the surface properties of mfps, the force-distance profiles of the interactions between thin mfp (i.e. mfp-1, mfp-3 or mfp-5) films and four different surface chemistries, namely mica, silicon dioxide, polymethylmethacrylate and polystyrene, were measured by an SFA. The results indicate that the adhesion was exquisitely dependent on the mfp tested, the substrate surface chemistry and the contact time. Such studies are essential for understanding the adhesive versatility of mfps and related/similar adhesion proteins, and for translating this versatility into a new generation of coatings and (including <I>in vivo</I> ) adhesive materials. </P>
Mussel foot protein-1 (mcfp-1) interaction with titania surfaces
Hwang, Dong Soo,Harrington, Matthew J.,Lu, Qingye,Masic, Admir,Zeng, Hongbo,Waite, J. Herbert The Royal Society of Chemistry 2012 Journal of materials chemistry Vol.22 No.31
<P>Marine mussels utilize a variety of DOPA-rich proteins for purposes of underwater adhesion, as well as for creating hard and flexible surface coatings for their tough and stretchy byssal fibers. In the present study, moderately strong, yet reversible wet adhesion between the protective mussel coating protein, mcfp-1, and amorphous titania was measured with a surface force apparatus (SFA). In parallel, resonance Raman spectroscopy was employed to identify the presence of bidentate DOPA–Ti coordination bonds at the TiO<SUB>2</SUB>–protein interface, suggesting that catechol–TiO<SUB>2</SUB> complexation contributes to the observed reversible wet adhesion. These results have important implications for the design of protective coatings on TiO<SUB>2</SUB>.</P> <P>Graphic Abstract</P><P>Moderately strong, yet reversible wet adhesion between mussel coating protein and titania was measured with a SFA and Raman spectroscopy. <IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=c2jm32439c'> </P>
Adhesion mechanism in a DOPA-deficient foot protein from green mussels
Hwang, Dong Soo,Zeng, Hongbo,Lu, Qingye,Israelachvili, Jacob,Waite, J. Herbert The Royal Society of Chemistry 2012 SOFT MATTER Vol.8 No.20
<P>The holdfast or byssus of Asian green mussels, <I>Perna viridis</I>, contains a foot protein, pvfp-1, that differs in two respects from all other known adhesive mussel foot proteins (mfp): (1) instead of the hallmark <SMALL>L</SMALL>-3,4-dihydroxyphenylalanine (DOPA) residues in mfp-1, for example, pvfp-1 contains C<SUP>2</SUP>-mannosyl-7-hydroxytryptophan (Man7OHTrp). (2) In addition, pvfp-1 chains are not monomeric like mfp-1 but trimerized by collagen and coiled-coil domains near the carboxy terminus after a typical domain of tandemly repeated decapeptides. Here, the contribution of these peculiarities to adhesion was examined using a surface forces apparatus (SFA). Unlike previously studied mfp-1s, pvfp-1 showed significant adhesion to mica and, in symmetric pvfp-1 films, substantial cohesive interactions were present at pH 5.5. The role of Man7OHTrp in adhesion is not clear, and a DOPA-like role for Man7OHTrp in metal complexation (<I>e.g.</I>, Cu<SUP>2+</SUP>, Fe<SUP>3+</SUP>) was not observed. Instead, cation–π interactions with low desolvation penalty between Man7OHTrp and lysyl side chains and conformational changes (raveling and unraveling of collagen helix and coiled-coil domains) are the best explanations for the strong adhesion between pvfp-1 monomolecular films. The strong adhesion mechanism induced by cation–π interactions and conformational changes in pvfp-1 provides new insights for the development of biomimetic underwater adhesives.</P> <P>Graphic Abstract</P><P>Molecular interactions of a DOPA-deficient foot protein from green mussels, pvfp-1, were measured using a surface forces apparatus (SFA). The strong adhesion mechanism induced by cation–π interactions and conformational changes in pvfp-1 provides new insights for the development of biomimetic underwater adhesives. <IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=c2sm25173f'> </P>