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010   $a3-319-06031-7
024 7 $a10.1007/978-3-319-06031-6
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035   $a(EBL)1731096
035   $a(OCoLC)883570917
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035   $a(PQKBTitleCode)TC0001237416
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035   $a(DE-He213)978-3-319-06031-6
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035   $a(EXLCZ)993710000000114379
100   $a20140512d2014      u|         0
101 0 $aeng
135   $aur|n|---|||||
181   $ctxt
182   $cc
183   $acr
200 10$aAdhesive Interactions of Mussel Foot Proteins /$fby Jing Yu
205   $a1st ed. 2014.
210  1$aCham :$cSpringer International Publishing :$cImprint: Springer,$d2014.
215   $a1 online resource (79 p.)
225 1 $aSpringer Theses, Recognizing Outstanding Ph.D. Research,$x2190-5053
300   $aDescription based upon print version of record.
311   $a3-319-06030-9 
320   $aIncludes bibliographical references at the end of each chapters and index.
327   $aMussel adhesion -- Surface Interactions in Biological Systems -- Effects of interfacial redox in mussel adhesive protein films on mica -- Antioxidant is a Key Factor in Mussel Protein Adhesion -- Hydrophobic enhancement of Dopa-mediated adhesion in a mussel foot protein -- Learning from the pieces: the adhesion of mussel-inspired peptides.
330   $aWater and moisture undermine strong adhesion to polar surfaces. Marine mussels, however, achieve durable underwater adhesion using a suite of proteins that are peculiar in having high levels of 3, 4-dihydroxyphenylalanine (Dopa). Mussel adhesion has inspired numerous studies on developing the next generation of wet adhesives. This thesis presents recent progress in understanding the basic surface and intermolecular interactions employed by mussels to achieve strong and durable wet adhesion. The surface forces apparatus (SFA) and various other techniques were applied to measure the interactions between mussel foot protein-3 fast (Mfp-3 fast) and the model substrate, mica, as well as the interactions between various mussel adhesive proteins. The results in this thesis show that Dopa plays an essential role in mussel adhesion, and that mussels delicately control the interfacial redox environment to achieve strong and durable Dopa mediated adhesion. The interplay between Dopa and hydrophobic interactions is also evident in mussel adhesion.
410  0$aSpringer Theses, Recognizing Outstanding Ph.D. Research,$x2190-5053
606   $aBiochemical engineering
606   $aMaterials?Surfaces
606   $aThin films
606   $aBiomedical engineering
606   $aBiomaterials
606   $aBiochemical Engineering$3https://scigraph.springernature.com/ontologies/product-market-codes/C12029
606   $aSurfaces and Interfaces, Thin Films$3https://scigraph.springernature.com/ontologies/product-market-codes/Z19000
606   $aBiomedical Engineering and Bioengineering$3https://scigraph.springernature.com/ontologies/product-market-codes/T2700X
606   $aBiomaterials$3https://scigraph.springernature.com/ontologies/product-market-codes/Z13000
615  0$aBiochemical engineering.
615  0$aMaterials?Surfaces.
615  0$aThin films.
615  0$aBiomedical engineering.
615  0$aBiomaterials.
615 14$aBiochemical Engineering.
615 24$aSurfaces and Interfaces, Thin Films.
615 24$aBiomedical Engineering and Bioengineering.
615 24$aBiomaterials.
676   $a594.4
700   $aYu$b Jing$4aut$4http://id.loc.gov/vocabulary/relators/aut$01061949
801  0$bMiAaPQ
801  1$bMiAaPQ
801  2$bMiAaPQ
906   $aBOOK
912   $a9910298643903321
996   $aAdhesive Interactions of Mussel Foot Proteins$92521563
997   $aUNINA