Selectivity and efficiency of enzymes can be fruitfully exploited in peptide chemistry for amide bond formation1, protection/deprotection strategies2, targetted modifications of side chains and also for selective cleavage of linkers in solid phase synthesis3.
Recent advances in applied biocatalysis enable the enzymatic peptide synthesis in rather extreme non conventional conditions, ranging from organic media, substrates anchored on solid supports and substrates mainly undissolved in nearly solvent-less systems4. Moreover, the technological advances in enzyme discovery and engineering have led to a broad range of efficient and selective enzymes to be used at lab scale.
Examples of how different „non conventional“ synthetic methodologies can match various peptide synthetic purposes will be presented. In a number of cases, translating an enzymatic reaction into an efficient biocatalysed process of practical applicability still remains a major bottleneck that hampers the full exploitation of the catalytic potential of enzymes. The use of computational tools, as modelling and statistics, will be discussed in the perspective of a more rational and effective exploitation of the technological and scientific advances in the field of applied biocatalysis, with particular regard to the field of peptide chemistry.
