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Abstract
Hee Young Yoo1,*, Mihaela Iordachescu1,*, Jun Huang2, Elise Hennebert3,4, Sangsik Kim5, Sangchul Rho6, Mathias Foo7, Patrick Flammang3, Hongbo Zeng2, Daehee Hwang6,8, J. Herbert Waite9 & Dong Soo Hwang1,5
1 Division of Integrative Biosciences and Biotechnology, Pohang University of Science and Technology, Pohang 37673, Republic of Korea. 2 Department of Chemical and Materials Engineering, University of Alberta, Edmonton, Alberta, Canada T6G 2V4. 3 Laboratory of Biology of Marine Organisms and Biomimetics, Research Institute for Biosciences, University of Mons, 7000 Mons, Belgium. 4 Laboratory of Cell Biology, Research Institute for Biosciences, University of Mons, 7000 Mons, Belgium. 5 School of Environmental Science and Engineering, Pohang University of Science and Technology, Pohang 37673, Republic of Korea. 6 Center for Plant Aging Research, Institute for Basic Science (IBS), Daegu 42988, Republic of Korea. 7 School of Engineering, University of Warwick, Coventry CV4 7AL, UK. 8 Department of New Biology, DGIST, Daegu 42988, Republic of Korea. 9 Department of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, California 93106, USA. * These authors contributed equally to this work.
Correspondence to : Dong Soo Hwang
Abstract
The byssal threads of the fan shell Atrina pectinata are non-living functional materials intimately associated with living tissue, which provide an intriguing paradigm of bionic interface for robust load-bearing device. An interfacial load-bearing protein (A. pectinata foot protein-1, apfp-1) with L-3,4-dihydroxyphenylalanine (DOPA)-containing and mannose-binding domains has been characterized from Atrina’s foot. apfp-1 was localized at the interface between stiff byssus and the soft tissue by immunochemical staining and confocal Raman imaging, implying that apfp-1 is an interfacial linker between the byssus and soft tissue, that is, the DOPA-containing domain interacts with itself and other byssal proteins via Fe3+-DOPA complexes, and the mannose-binding domain interacts with the soft tissue and cell membranes. Both DOPA- and sugar-mediated bindings are reversible and robust under wet conditions. This work shows the combination of DOPA and sugar chemistry at asymmetric interfaces is unprecedented and highly relevant to bionic interface design for tissue engineering and bionic devices.
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