Peptidomimetics via modifications of amino acids and peptide bonds

TLDR: This work reviews recent developments in peptidomimetics that are formed via heteroatom replacement within the native amino acid backbone through structural features, utility and preparative methods.

Abstract: Peptidomimetics represent an important field in chemistry, pharmacology and material science as they circumvent the limitations of traditional peptides used in therapy. Self-structural organizations such as turns, helices, sheets and loops can be accessed by chemical modifications of amino acids or peptides. In-depth structural and conformational analysis and structure–activity relationships (SAR) offer a way to establish peptidomimetic libraries. Herein, we review recent developments in peptidomimetics that are formed via heteroatom replacement within the native amino acid backbone. Each sub-section describes structural features, utility and preparative methods.