2010
DOI: 10.1007/s00253-010-2913-8
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Protein-based underwater adhesives and the prospects for their biotechnological production

Abstract: Biotechnological approaches to practical production of biological protein-based adhesives have had limited success over the last several decades. Broader efforts to produce recombinant adhesive proteins may have been limited by early disappointments. More recent synthetic polymer approaches have successfully replicated some aspects of natural underwater adhesives. For example, synthetic polymers, inspired by mussels, containing the catecholic functional group of 3,4-L-dihydroxyphenylalanine adhere strongly to … Show more

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Cited by 93 publications
(76 citation statements)
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“…In addition, fp-151 showed better adsorption and similar adhesion force, compared to recombinant fp-5, and its adhesive strength (∼0.8 MPa on cowhide, ∼1.1 MPa on aluminum, and ∼1.8 MPa on poly(methyl methacrylate (PMMA) (Plexiglas)) is always largely in excess of that of the commercially available fibrin glue Tisseel. The recombinant fusion proteins, marketed in milligram quantities (Kollodis, Inc), are less expensive than extracted MAPs (Cell-Tak) [10,96]. Recently, fp-151 was successfully produced in insect cells (Table 12.2) [96].…”
Section: Productionmentioning
confidence: 99%
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“…In addition, fp-151 showed better adsorption and similar adhesion force, compared to recombinant fp-5, and its adhesive strength (∼0.8 MPa on cowhide, ∼1.1 MPa on aluminum, and ∼1.8 MPa on poly(methyl methacrylate (PMMA) (Plexiglas)) is always largely in excess of that of the commercially available fibrin glue Tisseel. The recombinant fusion proteins, marketed in milligram quantities (Kollodis, Inc), are less expensive than extracted MAPs (Cell-Tak) [10,96]. Recently, fp-151 was successfully produced in insect cells (Table 12.2) [96].…”
Section: Productionmentioning
confidence: 99%
“…Recombinant DNA technology has been used in order to obtain large quantities of marine adhesive proteins (see [10,18,52] for review). Attempts to produce recombinant forms of MAPs started in the early 1990s with the expression, production, and purification of complete fp-1 and of synthetic fp-1 protein analogs consisting of 6-20 repeats of the consensus fp-1 decapeptide (Ala-Lys-Pro-Ser-Tyr-Pro-Pro-Thr-Tyr-Lys) in the yeast Saccharomyces cerevisiae or in the bacterium Escherichia coli [25,53].…”
Section: Productionmentioning
confidence: 99%
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