ausblenden:
Schlagwörter:
SOLID-PHASE SYNTHESIS; FARNESYL-PROTEIN TRANSFERASE; PROTECTING GROUP TECHNIQUES; ORGANIC-SYNTHESIS; HEPTYL ESTERS; CARBOHYDRATE-RECOGNITION; CHEMOENZYMATIC SYNTHESIS; NUCLEOPEPTIDE FRAGMENT; CELLULAR-REGULATION
Chemistry; enzymes; peptide conjugates; protecting groups; bioorganic chemistry; enzyme catalysts;
Zusammenfassung:
Glyco-, phospho-, nucleo- and lipoproteins play key roles in biological signalling cascades, by which chemical signals are passed across the cell membrane and further to the cell nucleus. For the study of the biological phenomena associated with these protein conjugates, structurally well-defined peptides containing the characteristic linkage region of the peptide backbone with the carbohydrate, the Lipid or the phosphoric acid ester can be applied advantageously. The multifunctionality and the pronounced acid- and base-lability of lipo-, phospho-, nucleo- and glycopeptides, however, renders their synthesis a formidable challenge to conventional or ganic synthesis. This review highlights the potential of enzymatic transformations, in particular for the removal of protecting groups, as central techniques for the construction of complex and sensitive biologically relevant peptide conjugates under particularly mild conditions and with high selectivity.
