Structural diversity of bicyclic amino acids |
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Authors: | A Trabocchi D Scarpi A Guarna |
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Institution: | (1) Dipartimento di Chimica Organica “Ugo Schiff” and Laboratorio di Progettazione, Sintesi e Studio di Eterocicli Bioattivi (HeteroBioLab), Università degli Studi di Firenze, Polo Scientifico e Tecnologico, Sesto Fiorentino, Firenze, Italy |
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Abstract: | Summary. Over the years biomedical research has been constantly oriented towards the development of new therapeutics based on bioactive
peptides and their analogues. In particular, the generation of compounds having structures and functions similar to bioactive
peptides, named “peptidomimetics”, raised much interest among organic and medicinal chemists due to the possibility by using
such compounds to improve both potency and stability of peptidic lead compounds. In the context of this research area, unnatural
amino acids are of great interest in drug discovery, and their use as new building blocks for the development of peptidomimetics
with high diversity level and possessing high-ordered structures is of special interest. In particular, medicinal chemistry
has taken advantage of the use of amino acid homologues and of cyclic and polycyclic templates to introduce elements of diversity
for the generation of new molecules as drug candidates. Bicyclic amino acids have been developed as reverse turn mimetics
and dipeptide isosteres, and the constraint imposed by their structures has been reported as a tool for controlling the conformational
preferences of modified peptides. Moreover, synthetic efforts have been driven to the generation of diverse structures based
on the modulation of ring size and scaffold decoration by suitable functional groups. Herein is reported an overview of different
classes of bicyclic amino acids, taking into account the strategies to achieve structurally diverse templates, and some implications
in medicinal chemistry are also disclosed.
Authors’ address: Antonio Guarna, Dipartimento di Chimica Organica “Ugo Schiff” and Laboratorio di Progettazione, Sintesi
e Studio di Eterocicli Bioattivi (HeteroBioLab), Università degli Studi di Firenze, Polo Scientifico e Tecnologico, Via della
Lastruccia 13, I-50019 Sesto Fiorentino, Firenze, Italy |
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Keywords: | : Scaffold – Peptide – Peptidomimetic – Drug design |
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