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Over the past two decades many reports have demonstrated the value of non-canonical amino acids (ncAA) as single bioactive molecules, scaffolds and building blocks for drug discovery, for probing protein function, as parts of bioactive peptides, for design of antibody-drug conjugates, and for design of new biomaterials. We have reviewed state-of-the art biocatalytic approaches to synthesise ncAAs, including metabolic engineering, and addressed recent advances made in the field of synthetic biology to allow direct incorporation of ncAAs in proteins. We have then focused on the role of ncAAs in modification and improvement of antimicrobial peptides (AMPs) and discussed how using orthogonal translation systems can contribute to more efficient synthesis of AMPs while simultaneously improving their bioavailability. Finally, we have addressed the latest achievements in application of ncAAs for the modification of anticancer peptides (ACP).

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