Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/5432
Title: Intrinsic surface-drying properties of bioadhesive proteins
Authors: Akdoğan, Yaşar
Wei, Wei
Huang, Kuo-Ying
Kageyama, Yoshiyuki
Danner, Eric W.
Miller, Dusty R.
Martinez Rodriguez, Nadine R.
Waite, J. Herbert
Han, Songi
Keywords: Dynamic nuclear polarization
EPR spectroscopy
Hydrophobic effect
Mussel foot proteins
Wet adhesion
Proteins
Publisher: John Wiley and Sons Inc.
Source: Akdoğan, 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.201406858
Abstract: Sessile 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.
URI: http://doi.org/10.1002/anie.201406858
http://hdl.handle.net/11147/5432
ISSN: 1433-7851
1433-7851
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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