Thesis title Enantioselective Chalcogen Bonding Catalysis

微生物产生铁载体，用于获取和储存铁。在真菌中，产生的大多数铁载体化合物属于异羟甲酸酯类。这种化学功能来源于L-鸟氨酸，它被N5-羟基化，然后N5-酰化生成双齿配体。最近的工作阐明了非核糖体多肽合成酶(NRPS)的分子编程，该酶负责铁的生物合成，铁是一种环状六肽铁载体。这种NRPS提供了通过化学合成和酶结构域的突变来生产铁铬支架的衍生物的令人兴奋的潜力。该项目旨在利用NRPS的灵活性，引入不同的肽基骨架和双正交手柄进行衍生化。新化合物具有作为抗生素和医学成像的潜在用途。

Microorganisms produce siderophores for acquisition and storage of iron. In fungi, the majority of siderophore compounds produced belong to the hydroxamate class. This chemical functionality originates from L-ornithine, which is N5-hydroxylated and subsequently N5-acylated to yield a bidentate ligand. Recent work has elucidated the molecular programming of the non-ribosomal peptide synthetase (NRPS) enzyme responsible for the biosynthesis of ferrichrome, a cyclic hexapeptide siderophore. This NRPS offers the exciting potential to produce derivatives of the ferrichrome scaffold through chemical synthesis and mutagenesis of the enzymatic domains. This project aims to exploit the flexibility of the NRPS to introduce different peptidyl backbones, and biorthogonal handles for derivatisation. Novel compounds have potential uses as antibiotics and in medical imaging.