Non-ribosomal peptide synthesis is a fascinating way in which nature assembles peptides in a stepwise manner without the involvement of the ribosome. This enzymatic assembly line produces many important natural products and these often contain a diverse range of amino acids not found in proteins: important examples are arylglycines, which are found in a range of antibiotic compounds that includes the glycopeptide antibiotics. In order to characterise and understand the biosynthesis of such natural products we need to be able to access peptides intermediates: additionally, these must also be modified in such a way as to allow ligation to the biosynthetic machinery itself, as non-ribosomal peptide synthesis relies on the tethering of intermediates as thioesters to carrier protein domains. To address this need, we have developed a rapid route to glycopeptide precursor CoA conjugates based on Fmoc-chemistry that affords both high yields and excellent purities. This route allows the synthesis of peptide CoA-conjugates containing racemization-prone arylglycine residues: such residues have previously been inaccessible to peptide synthesis using Fmoc-type chemistry. We are also investigating other methods of synthesising peptides in a form appropriate for loading onto carrier proteins, and recent results of these investigations will be presented here.