Abstract
In contrast to peptide synthesis, peptide purification by high performance liquid chromatography (HPLC) cannot be easily varied in number and scale, which results in production restraints. Catch‐and‐release purification of peptides may help to ease HPLC‐related limitations and provides thus an alternative, allowing for fast protocols with great potential for parallelization and scale‐up. This work depicts a unique combination of base‐labile cleavable linkers with oxime‐based and hydrazone‐based ligation chemistry. For the first time, aminooxy or hydrazine functionalities are presented on site of the linker molecules. Aldehyde‐functionalized agarose beads are used for immobilization on the solid phase, allowing a rapid and high yielding purification protocol. In this experimental set‐up, many organic solvents or chaotropic reagents are accepted during immobilization, facilitating the dissolution of potentially hydrophobic or aggregation‐prone peptides. Feasibility of the system is demonstrated with six peptides ranging from 15 to 31 residues in length, including very hydrophobic and thus challenging sequences like the palmitoyl modified liraglutide and an aggregation prone beta‐amyloid fragment. Additionally, limitations of this system and the use of base‐labile linkers are discussed and demonstrated.
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Schedule a callMore From: Journal of peptide science : an official publication of the European Peptide Society
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