title: Intrinsic surface-drying properties of bioadhesive proteins.
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.
authors.affiliation: Department of Chemistry and Biochemistry, University of California Santa Barbara, Santa Barbara, CA 93106 (USA); İzmir Institute of Technology, Department of Materials Science and Engineering, İzmir, 35430 (Turkey).
authors.forename: Yasar
authors.initials: Y
authors.lastname: Akdogan
authors.forename: Wei
authors.initials: W
authors.lastname: Wei
authors.forename: Kuo-Ying
authors.initials: KY
authors.lastname: Huang
authors.forename: Yoshiyuki
authors.initials: Y
authors.lastname: Kageyama
authors.forename: Eric W
authors.initials: EW
authors.lastname: Danner
authors.forename: Dusty R
authors.initials: DR
authors.lastname: Miller
authors.forename: Nadine R
authors.initials: NR
authors.lastname: Martinez Rodriguez
authors.forename: J Herbert
authors.initials: JH
authors.lastname: Waite
authors.forename: Songi
authors.initials: S
authors.lastname: Han
mesh_terms: D000269:Adhesives / Q000737:chemistry*; D000327:Adsorption; D000818:Animals; D049872:Bivalvia / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D011506:Proteins / Q000737:chemistry*; D013499:Surface Properties
chemical_list: D000269:Adhesives; D011506:Proteins
keywords: EPR spectroscopy; dynamic nuclear polarization; hydrophobic effect; mussel foot proteins; wet adhesion