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• W1973701329 abstract "The covalent and non-covalent immobilization of growth factors such as recombinant human bone morphogenetic protein 2 (rhBMP-2) on metals and bone replacement materials in bioactive form is a recent development. Up to now the immobilization technology usually involved the chemical modification and activation of the biomaterial surface followed by attachment of the bioactive protein. Here we suggest an alternative method in which an affinity tag fused to an active protein will allow immobilization without additional chemistry. For biomaterials such as minerals, metals (titanium, steel, CoCrMo), glass ceramics, teflon and possibly bone and teeth ideal adhesion molecules would be the foot proteins (Mefps) of the mussel M. edulis which contain the rare amino acid dihydroxy phenylalanine (DOPA). Recently it could be shown by Messersmith's group that a single DOPA-molecule can be non-covalently bound to titanium dioxide surface with a dissociation energy of 22.2 kcal/mol (Lee, H.; Scherer, N. F.; Messersmith, P. B. Proc. Natl. Acad. Sci. U. S. A 2006, 103, 12999–13003).We therefore propose the DOPA-tag as a general and versatile affinity tag for the immobilization of proteins on biomaterials. Entwicklung eines universellen Affinitäts-Fusionstags (Poly-DOPA) zur Immobilisierung rekombinanter Proteine auf Biomaterialien. Die kovalente und nicht-kovalente Immobilisierung von Wachstumsfaktoren wie rekombinantem knochenmorphogenetischem Protein 2 (rhBMP-2) auf Metallen und Knochenersatzmaterialien in bioaktiver Form stellt eine kürzliche Entwicklung dar. Bis heute beinhaltet die Immobilisierungstechnik die chemische Modifikation und Aktivierung der Biomaterialoberfläche gefolgt von der Bindung des bioaktiven Proteins. Wir stellen hier eine alternative Technik vor, wobei ein an ein aktives Protein fusionierter Affinitäts-Tag, die Immobilisierung ohne zusätzliche Chemie erlaubt. Für Biomaterialien wie Minerale, Metalle (Titan, Stahl, CoCrMo), Glaskeramiken, Teflon und möglicherweise Knochen und Zähne würden Proteine aus dem Fuß (Mefps) der Muschel M. edulis, die die seltene Aminosäure Dihydroxyphenylalanine (DOPA) enthalten, ideale Adhäsionsmoleküle darstellen. Kürzlich konnte die Gruppe von Messersmith zeigen, daß ein einzelnes DOPA-Molekül nicht-kovalent an eine Titandioxidoberfläche mit einer Dissoziationsenergie von 22.2 kcal/mol (Lee, H.; Scherer, N. F.; Messersmith, P. B. Proc. Natl. Acad. Sci. U. S. A 2006, 103, 12999–13003) gebunden werden kann. Daher schlagen wir DOPA-Tags als allgemeine und vielseitige Affinitäts-Tags für die Immobilisierung von Proteinen auf Biomaterialien vor." @default.
• W1973701329 created "2016-06-24" @default.
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• W1973701329 date "2007-12-01" @default.
• W1973701329 modified "2023-09-29" @default.
• W1973701329 title "Development of an universal affinity fusion tag (Poly-DOPA) for immobilizing recombinant proteins on biomaterials" @default.
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• W1973701329 doi "https://doi.org/10.1002/mawe.200700247" @default.
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