Despite its importance for synthetic chemistry, selective introduction of halogens using conventional approaches often remains challenging, whereas biocatalysis offers excellent catalyst-controlled selectivity without requiring protecting groups. Hence halogenating enzymes increasingly attract attention for biocatalytic C-H functionalization.
The formylglycine generating enzyme (FGE) is a valuable tool for bioconjugation. It catalyzes the oxygen-dependent oxidation of a cysteine residue within the recognition sequence CXPXR in type-I-sulfatases to Cα-formylglycine (FGly).
Peptidomimetics retain the ability of their natural peptide counterparts to interact with biological targets while showing improved stability profiles and pharmacokinetic properties.
Cryptophycins are naturally occurring cytotoxins with great potential for chemotherapy. Since targeted therapy provides new perspectives for treatment of cancer, new potent analogues of cytotoxic agents containing functional groups for conjugation to homing devices are required.
Halogenated compounds are important building blocks for metal-catalyzed cross-coupling reactions, e.g. Suzuki-Miyaura cross-coupling (SMC), which gives access to biaryl motifs suitable for peptide cyclization & modification.
Gluten-related disorders are a complex group of diseases that involve the activation of the immune system triggered by the ingestion of gluten. Previous studies have pointed out that a smaller, proteolytic-resistant peptide fragment of gluten, gliadin, can self-assemble under different conditions in aqueous media that is believed to induce the immune system.
Protein-peptide interactions are essential for every living organism and hence are often related to many diseases. Consequently, these interactions can be systematically addressed to develop potential inhibitors. In order to use peptides as drugs, various modifications can be conducted to increase their bioactivity and stability and to synthesise tailor-made inhibitors, e. g. for tumour treatment.