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The Challenge of Conformational Isomerism in Cyclic Peptoids
Author(s) -
De Riccardis Francesco
Publication year - 2020
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/ejoc.201901838
Subject(s) - peptoid , peptidomimetic , chemistry , chirality (physics) , cyclic peptide , stereochemistry , peptide , biochemistry , chiral symmetry breaking , physics , quantum mechanics , nambu–jona lasinio model , quark
Peptoids ( N ‐substituted glycine oligomers) are an increasingly important class of peptidomimetic foldamers with conspicuous bioactivities, high degree of resistance to enzymatic degradation, and ability to form stable secondary structures. The intrinsic rigidity of their oligoamide framework (due to n →π*, side chains N C α –H ··· O=C n →σ*, and backbone C α –H ··· O=C interactions), can be magnified by cyclization to afford macrocyclic species with unexpected stereochemical, topological and biochemical attributes. In this minireview the implications of conformational chirality, a largely overlooked source of chirality in medium and large size cyclic peptoids, are addressed. The exploration of the unique structural and recognition properties of macrocyclic peptoid biomimetics unravels potential strategies for design and development of sequence‐defined (cyclo)oligomers where conformational isomerism is an issue.