Journal
AMINO ACIDS
Volume 39, Issue 3, Pages 671-683Publisher
SPRINGER WIEN
DOI: 10.1007/s00726-010-0488-4
Keywords
Laccase; Mussel adhesive proteins; Cross-link; Biomaterial; epsilon-Amino group
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Funding
- European Union
- Stryker Trauma GmbH (Schonkirchen)
- Aesculap AG & Co. KG (Tuttlingen)
- BSN medical GmbH & Co. KG (Hamburg)
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In order to design potential biomaterials, we investigated the laccase-catalyzed cross-linking between l-lysine or lysine-containing peptides and dihydroxylated aromatics. l-Lysine is one of the major components of naturally occurring mussel adhesive proteins (MAPs). Dihydroxylated aromatics are structurally related to 3,4-dihydroxyphenyl-l-alanine, another main component of MAPs. Mass spectrometry and nuclear magnetic resonance analyses show that the epsilon-amino group of l-lysine is able to cross-link dihydroxylated aromatics. Additional oligomer and polymer cross-linked products were obtained from di- and oligopeptides containing l-lysine. Potential applications in medicine or industry for biomaterials synthesised via the three component system consisting of the oligopeptide [Tyr-Lys](10), dihydroxylated aromatics and laccase are discussed.
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