Mussel adhesive proteins

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]. 

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. 

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,... 

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. 

In early studies, mussel adhesive protein-derived consensus sequences were synthesized in solution phase and covalently coupled to yield adhesive-mimetic polypeptides, such as a DOPA-containing polydecapeptide In related synthetic... 

No gelation was observed in the absence of catechol-containing 3,4-dihydroxystyrene. This polymer represents a simplified mimic of mussel adhesive proteins, utilizing catechol oxidation to induce gelation. Gatechol-containing polyurethane polymer adhesives XIX have also recently been reported. ... 

In addition to the mussel adhesive proteins, DOPA is found in polychaete sandcastle worm glue secretions, which are in situ forming multiprotein cements deployed during constmction of tube-shaped brick and mortar shelters built from particulates that are available in the sandcastle worm environment. These interesting protein cements have been characterized and have led to the recent emergence of first-generation biomimetic polymer adhesives. 

Abstract Aqueous biocompatible tribosystems are desirable for a variety of tissue-contacting medical devices. L-3,4-dihydroxyphenylalanine (DOPA) and lysine (K) peptide mimics of mussel adhesive proteins strongly interact with surfaces and may be useful for surface attachment of lubricating polymers in tribosystems. Here, we describe a significant improvement in lubrication properties of poly (dimethylsiloxane) (PDMS) surfaces when modified with PEG-DOPA-K. Surfaces were characterized by optical and atomic force microscopy, contact angle, PM-IRRAS, and X-ray photoelectron spectroscopy. Sudi surfaces, tested over the course of 200 rotations ( 8 m in length), maintained an extremely low friction coefficient (p) (0.03 0.00) compared to bare PDMS (0.98 0.02). These results indicate... 

Dalsin JL, Hu BH, Lee BP, Messersmith PB. Mussel adhesive protein mimetic polymers for the preparation of nonfouling surfaces. J Am Chem Soc 2003 125 4253-4258. 

Chemical reduction is the most frequently applied method for the preparation of silver nanoparticles as stable, colloidal dispersions in water or organic solvents. However, a number of alternative green chemistry synthesis routes have been reported. Inspired by mussel adhesive proteins, a novel functional polyurethane based on hydrolyzable tannins that contain a number of catechol groups was... 

To date, most knowledge on adhesive systems has been obtained by analyzing and nurnicking the adhesive proteins of mussels (Silverman and Roberto, 2007). Mussels anchor themselves strongly to a surface by the byssus. The byssus secretes proteinaceous threads ending in adhesive plaques (Fig. 2.2(a)). These plaques comprise among other components five polyphenohc foot proteins (fp2-6) and an accessory protein lp-1 (Zhao and Waite, 2006) (Fig. 2.2(b)). These six proteins are also known as mussel adhesive proteins (MAPs) and share as a common feature the presence of DOPA... 

Hwang, D.S., Sim, S.B., Cha, H.J., 2007b. Cell adhesion biomaterial based on mussel adhesive protein fused with RGD peptide. Biomaterials 28, 4039—4046. 

Hwang, D.S., Waite, J.H., Tirrell, M., 2010. Promotion of osteoblast proliferation on complex coacervation-based hyaluronic acid — recombinant mussel adhesive protein coatings on titanium. Biomaterials 31, 1080—1084. 

---