Mussel adhesion

Mussel adhesive protein (MAP) is a 130-kDa protein produced by the blue mussel Mytilus edulis), which provides strong adhesion to submerged surfaces. MAP films were prepared by drying and stored under nitrogen atmosphere. These films showed twice the adhesion strength of polycarbophil when tested on porcine duodenum in vitro [95]. 

Lee H, Scherer NF, Messersmith PB. Single-molecule mechanics of mussel adhesion. Proc Natl Acad Sci USA 2006 103 12999-13003. 

Waite J, Andersen N, Jewhurst S, Sun C. Mussel adhesion finding the tricks worth mimicking. J Adhes 2005 81 297-317. 

Tonegawa et al. (2004) created a cationic polylysine with a tetrapeptide end sequence (glycine-tyrosine-glycine-lysine), which is a motif common to the consensus sequences of mussel adhesive proteins. They then cross-linked this with the anionic polysaccharide, gellan, enzymatically. The polyionic complexation between the cationic peptide and the anionic polysaccharide formed a hybrid fiber at the aqueous solution interface that, when cross-linked, mimicked the byssus gel that marine mussels use to adhere to surfaces, despite the presence of water and salt. 

Development of a Microbial System for Production of Mussel Adhesive... 

Isolation and Characterization of cDNA Clones Encoding the Poly-phenolic Protein. Characterization of the primary amino acid sequence of the mussel adhesive protein has been hindered by the large size of the protein and the repetitiveness of the amino acids. In such cases, the practical (and perhaps only) approach for determining the complete amino acid sequence is to clone DNA sequences encoding the protein and to deduce the amino acid sequence from the genetic code carried by that DNA. To accomplish this, we obtained mRNA from mussels and synthesized cDNA in vitro. 

Best understood of the invertebrate adhesive-mediated attachment mechanisms is that of the common blue mussel, Myiilus edulis, and its close relative, Mytilus californianus L. The mechanism includes the byssus, an acellular proteinaceous organ produced by glands inside the mussel, combined with a delivery system that secretes the byssus efficiently underwater. The protein that is the functional unit of the adhesive mixture was first purified from the gland where it originates and characterized by Waite and Tanzer (i). Called mussel adhesive protein (MAP), it is a high molecular weight (120,000 10,000 MW) basic protein,... 

Even the aggregation of globular adhesion proteins to specific supramolecular structures observed in barnacle cement may be speculated to be a general theme in aquatic organisms, since similar structures have been found in mussel adhesive. 

Hwang, D.S., Yoo, H.J., Jun, J.H. et al. (2004) Expression of fimctional recombinant mussel adhesive protein Mgfp-5 in Escherichia coli. Applied aiulEnvironmental Microbiology, 70,3352-3359. 

Hwang, D.S., Gim, Y. and Cha, H.J. (2005) Expression of functional recombinant mussel adhesive protein t5rpe 3 A in Escherichia coli. Biotechnology Progress, 21,965-970. 

Kim, D., Hwang, D.S., Kang, D.G. et al. (2008) Enhancement of mussel adhesive protein production in Escherichia coli by co-expression of bacteritd hemoglobin. Biotechnology Progress, 24,663-666. 

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