Laccase-catalyzed cross-linking of amino acids and peptides with dihydroxylated aromatic compounds.
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.
Institute of Microbiology, Ernst-Moritz-Arndt-University Greifswald, Friedrich-Ludwig-Jahn Strasse 15, 17487, Greifswald, Germany. annett.mikolasch@uni-greifswald.de
Annett
A
Mikolasch
Veronika
V
Hahn
Katrin
K
Manda
Judith
J
Pump
Nicole
N
Illas
Dirk
D
Gördes
Michael
M
Lalk
Manuela
M
Gesell Salazar
Elke
E
Hammer
Wolf-Dieter
WD
Jülich
Stephan
S
Rawer
Kerstin
K
Thurow
Ulrike
U
Lindequist
Frieder
F
Schauer
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry*; D002384:Catalysis; D003432:Cross-Linking Reagents / Q000737:chemistry; D005656:Fungal Proteins / Q000737:chemistry; D006841:Hydrocarbons, Aromatic / Q000737:chemistry*; D042845:Laccase / Q000737:chemistry*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry; D055494:Pycnoporus / Q000201:enzymology
D000596:Amino Acids; D003432:Cross-Linking Reagents; D005656:Fungal Proteins; D006841:Hydrocarbons, Aromatic; D010455:Peptides; D011506:Proteins; C037403:adhesive protein, mussel; D042845:Laccase