✍ Scribed by Irene Coin
No coin nor oath required. For personal study only.
After about one century of peptide chemistry, the main limitation to the accessibility of peptides and proteins via chemosynthesis is the arising of folding and aggregation phenomena. This is true not only for sequences above a critical length but also for several biologically relevant substrates that are relatively short yet form either highly folded structures (e.g. WW domains) or fibrils and aggregates after final deprotection (β‐amyloid peptide). Such so‐called difficult sequences may be more easily obtained via their corresponding depsipeptides (O‐acyl isopeptides), ester isomers that are often easier to assemble and purify, and are smoothly converted to the parent amides under mild conditions. The depsipeptide method is the most recent technique to improve the outcome of difficult syntheses, applicable to sequences containing residues of serine or threonine. A brief overview is presented about chemical aspects of the method, the steps that have been undertaken for its optimization, and the evaluation of its efficiency. Further applications of analogous principles to other critical topics in peptide synthesis such as condensation of peptide segments and solid‐phase synthesis of naturally occurring cyclodepsipeptides are addressed as well. Copyright © 2010 European Peptide Society and John Wiley & Sons, Ltd.
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