Laccase-catalyzed cross-linking of amino acids and peptides with dihydroxylated aromatic compounds

Abstract

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.

Amine‐Functionalized Amino Acid‐based Ionic Liquids as Efficient and High‐Capacity Absorbents for CO2

“…L ‐Lysine is the most important component of naturally occurring mussel adhesive proteins, and has been found in the laccase‐catalyzed cross‐linking reaction with hydroquinone derivatives 156. Hahn et al 157. synthesized unprotected L ‐phenylalanine derivatives by an innovative enzymatic process that uses laccases isolated from P. cinnabarinus and M. thermophila .…”

“…In the presence of laccases, the derivatives of unprotected amino acids (e.g., L ‐tryptophan and L ‐phenylalanine) are produced; by contrast, use of sodium iodate results in very slow product formation and negligible product yields. Therefore, enzymatic catalysis is more effective than inorganic chemical catalysis in the synthesis of amino acid derivatives with 2,5‐dihydroxyacetophenone 157…”

Laccase‐catalyzed, Phytochemical‐mediated Protein Crosslinking Conjugates

“…On the other hand, combination of advanced analytical methods such as Mass Spectrometry (MS) [25,27,29,36], high performance liquid chromatography [26,29], and fluorescence spectroscopy [33,34,35] were also reportedly applied to investigate the laccase-catalyzed, phytochemical-mediated protein crosslinking. For instance, in a tandem MS study, the finding helped to provide supporting evidence as to the functional roles of tyrosine and cysteine residues in the crosslinked mechanism [36].…”

“…In terms of the catalytic mechanism, the current available literature suggesting that the laccase-catalyzed protein crosslinking is formed via amino residues such as tyrosine, cysteine and lysine [27,36]. However, the possibility of laccase enzyme to activate other amino residues could not be ruled out, especially considering the fact that laccase is widely described as an enzyme with broad substrate specificity.…”

Laccase

“…11 (F) Proteins containing large amounts of lysine residues can react with dihydroxylated aromatics to form a three-dimensional network through oxidative cross-links in the presence of laccase. 12 …”