Inter- and intramolecular adhesion mechanisms of mussel foot proteins

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ter- and intramolecular adhesion mechanisms of mussel foot proteins 1

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KAN YaJing , WEI ZhiYong , TAN QiYan & CHEN YunFei 1

1*

Jiangsu Key Laboratory for Design and Manufacture of Micro-Nano Biomedical Instruments, and School of Mechanical Engineering, 2

Southeast University, Nanjing 211189, China; School of Mechanical Engineering, Nanjing Institute of Technology, Nanjing 211167, China Received November 9, 2019; accepted February 18, 2020; published online May 21, 2020

Mussel foot proteins (Mfps) secreted in the byssal plaque of marine mussels are widely researched for their relevance to mussel adhesion in water. As the abundant residue in the amino acid sequences of major adhesive proteins, 3,4-dihydroxyphenylalanine (Dopa) or its catecholic moiety plays a key role in both Mfp binding to surface and cohesive cross-linking of Mfps in byssal plaques. The binding performance of an Mfp significantly depends on the content and redox state of Dopa, whereas the types of interaction vary in line with different surface chemistries and pH conditions. Thorough understanding of mussel adhesion from a molecular perspective is crucial to promote the application of synthetic mussel-bionic adhesives. This article presents a brief review of the research progress on the adhesion mechanisms of Mfps, which further emphasizes the contributions of Dopamediated interactions and considers other amino acids and factors. The involved inter- and intramolecular interactions are responsible for not only the diverse adhesion capacities of an adhesive byssal plaque as mussel’s adhesion precursor but also the formation and properties of the plaque structure. mussel foot protein, adhesion mechanism, Dopa, catechol, surface forces apparatus Citation:

Kan Y J, Wei Z Y, Tan Q Y, et al. Inter- and intramolecular adhesion mechanisms of mussel foot proteins. Sci China Tech Sci, 2020, 63, https://doi. org/10.1007/s11431-019-1541-8

1 Introduction Marine mussel is well known for its firm attachment to various substrates in wet and highly saline environments. In the presence of water, strong attraction at the attachment interface of traditional adhesives, usually known as van der Waals force, can be weakened dramatically [1]. The unique adhesion abilities of mussels are great inspiring sources for development of biomimetic functional materials, offering a solution to working against humidity. When approaching a solid surface in daily life, a mussel has hundreds of holdfast byssal threads that reach out from its foot, with their proximal ends jointed with a stem-like structure. At the distal end of each byssal thread, an adhesive plaque anchors on the *Corresponding author (email: [email protected])

surface, directly conducting mussel adhesion by joint attachment from tens of them. A tenacity test on a Mytilus californianus with only nine byssal threads adhering to a rock in seawater shows a normal attachment force of 15 N [2]. The adhesive capability may become slightly weaker on polymeric surfaces compared with other surfaces but remains su