Allowing stepwise addition of protected amino acids on an insoluble polymer support, solid phase peptide synthesis (SPPS) facilitates access to D-polypeptide chains. Fmoc-protected amino acids have gained popularity over the past two decades as they facilitate the use of milder cleavage conditions. Efficient reagents that allow high conversion of amino acid coupling have been reported. The systematic nature of SPPS has also led to automated systems. When paired with microwave irradiation, each amino acid coupling cycle can be performed in four minutes. Recently, a fully automated system for SPPS, where the assembly is complete in a flow system has been developed, yielding complete coupling cycles in less than two minutes, and a full protein up to 164 residues has been assembled. However, a major drawback is its requirement for a large excess of amino acids (6-60 equivalents), a major financial burden when it comes to D-polypeptide synthesis. This is especially the case when the target proteins contain diastereomeric D-isoleucine, which is significantly higher in cost than other building blocks.