sin A Peptide expression

ven pr en e n th ry. U tide s ro itio duc yield of peptide-fusions and the intrinsic chemical characteristics of the peptides, indicating that this sys-sed in interac actions molec trate s s [15– quali of nineteen of the 20 naturally occurring amino acids and the asso-ciated difficulties in purification of the isomers set practical limits to peptide lengths in library synthesis [23,24]. Sometimes peptide sequences are restricted due to steric clash of adjacent amino acids with bulky chemical catalysts or intermolecular aggregation which ners such as glutathione-S-transferase [29], maltose binding pro-tein [30], and thioredoxin [31] being the three most widely used fusions. While fusion proteins often promote production, this method can be time consuming and requires post expression pro-tease processing and purification of the peptide from the protease. However, the addition of fusion partners has resulted in the improvement of the overall yields by enhancing solubility of the peptide of choice. We report a method that allows robust expression of a geneti-cally encoded peptide library that addresses the issues of purity, yield, length of the purified peptide, and batch-to-batch variabilit