Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/5432
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dc.contributor.authorAkdoğan, Yaşar-
dc.contributor.authorWei, Wei-
dc.contributor.authorHuang, Kuo-Ying-
dc.contributor.authorKageyama, Yoshiyuki-
dc.contributor.authorDanner, Eric W.-
dc.contributor.authorMiller, Dusty R.-
dc.contributor.authorMartinez Rodriguez, Nadine R.-
dc.contributor.authorWaite, J. Herbert-
dc.contributor.authorHan, Songi-
dc.date.accessioned2017-04-28T08:11:21Z
dc.date.available2017-04-28T08:11:21Z
dc.date.issued2014-10
dc.identifier.citationAkdoğan, Y., Wei, W., Huang, K.-Y., Kageyama, Y., Danner, E. W., Miller, D. R., Martinez Rodriguez, N. R., Waite, J. H., and Han, S. (2014). Intrinsic surface-drying properties of bioadhesive proteins. Angewandte Chemie - International Edition, 53(42), 11253-11256. doi:10.1002/anie.201406858en_US
dc.identifier.issn1433-7851
dc.identifier.issn1433-7851-
dc.identifier.urihttp://doi.org/10.1002/anie.201406858
dc.identifier.urihttp://hdl.handle.net/11147/5432
dc.description.abstractSessile marine mussels must "dry" underwater surfaces before adhering to them. Synthetic adhesives have yet to overcome this fundamental challenge. Previous studies of bioinspired adhesion have largely been performed under applied compressive forces, but such studies are poor predictors of the ability of an adhesive to spontaneously penetrate surface hydration layers. In a force-free approach to measuring molecular-level interaction through surface-water diffusivity, different mussel foot proteins were found to have different abilities to evict hydration layers from surfaces - a necessary step for adsorption and adhesion. It was anticipated that DOPA would mediate dehydration owing to its efficacy in bioinspired wet adhesion. Instead, hydrophobic side chains were found to be a critical component for protein-surface intimacy. This direct measurement of interfacial water dynamics during force-free adsorptive interactions at solid surfaces offers guidance for the engineering of wet adhesives and coatings. Home and dry underwater: Repulsive hydration forces hinder wet adhesion in the absence of applied external forces. The direct measurement of hydration-water dynamics by NMR relaxometry at 10 GHz revealed that the most hydrophobic mussel adhesive protein, and not the most enriched with 3,4-dihydroxyphenylalanine, effectively dries the surface and overcomes repulsive hydration forces to adsorb spontaneously to surfaces in preparation for adhesion.en_US
dc.description.sponsorshipNational Science Foundation (NSF) through the MRSEC Program (DMR-1121053); MRSEC Program of the NSF (DMR-1121053); NIH Innovator Award; US National Institutes of Health (R01 DE018468); Human Frontiers of Science Programen_US
dc.language.isoenen_US
dc.publisherJohn Wiley and Sons Inc.en_US
dc.relation.ispartofAngewandte Chemie - International Editionen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectDynamic nuclear polarizationen_US
dc.subjectEPR spectroscopyen_US
dc.subjectHydrophobic effecten_US
dc.subjectMussel foot proteinsen_US
dc.subjectWet adhesionen_US
dc.subjectProteinsen_US
dc.titleIntrinsic surface-drying properties of bioadhesive proteinsen_US
dc.typeArticleen_US
dc.authoridTR180857en_US
dc.institutionauthorAkdoğan, Yaşar-
dc.departmentİzmir Institute of Technology. Materials Science and Engineeringen_US
dc.identifier.volume53en_US
dc.identifier.issue42en_US
dc.identifier.startpage11253en_US
dc.identifier.endpage11256en_US
dc.identifier.wosWOS:000343751100024en_US
dc.identifier.scopus2-s2.0-84941088422en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.identifier.doi10.1002/anie.201406858-
dc.identifier.pmid25168789en_US
dc.relation.doi10.1002/anie.201406858en_US
dc.coverage.doi10.1002/anie.201406858en_US
dc.identifier.wosqualityQ1-
dc.identifier.scopusqualityQ1-
item.grantfulltextopen-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextWith Fulltext-
item.languageiso639-1en-
item.openairetypeArticle-
item.cerifentitytypePublications-
crisitem.author.dept03.09. Department of Materials Science and Engineering-
Appears in Collections:Materials Science and Engineering / Malzeme Bilimi ve Mühendisliği
PubMed İndeksli Yayınlar Koleksiyonu / PubMed Indexed Publications Collection
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection
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