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Formylglycine-generating enzymes are of increasing interest in the field of bioconjugation chemistry. They catalyze the site-specific oxidation of a cysteine residue to the aldehyde-containing amino acid C -formylglycine (FGly). This non-canonical residue can be generated within any desired target protein and can subsequently be used for bioorthogonal conjugation reactions. The prototypic formylglycine-generating enzyme (FGE) and the iron-sulfur protein AtsB display slight variations in their recognition sequences. We designed specific tags in peptides and proteins that were selectively converted by the different enzymes. Combination of the different tag motifs within a single peptide or recombinant protein enabled the independent and consecutive introduction of two formylglycine residues and the generation of heterobifunctionalized protein conjugates.

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Polymer fibers are one of the main substances used for the reinforcement of plastic composites. Surface modification of aramid fiber was performed by direct fluorination. The crystallinity and the decomposition temperature of the modified fiber were increased. Scanning electron microscope shows that the roughness increases in the modified fiber. Composites were prepared by using modified and unmodified fibers. It was shown that the mechanical and thermal properties increase for modified fiber reinforcing composites. To reduce the fiber degradation or breakdown, composites were prepared by solution casting method. POLYM. COMPOS., 28:462–469, 2007. © 2007 Society of Plastics Engineers

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