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Solid‐State Conformational Flexibility at Work: Zipping and Unzipping within a Cyclic Peptoid Single Crystal
Author(s) -
Meli Alessandra,
Macedi Eleonora,
De Riccardis Francesco,
Smith Vincent J.,
Barbour Leonard J.,
Izzo Irene,
Tedesco Consiglia
Publication year - 2016
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201511053
Subject(s) - peptoid , peptidomimetic , chemistry , flexibility (engineering) , crystallography , transformation (genetics) , crystal engineering , solid state , single crystal , crystal structure , stereochemistry , peptide , supramolecular chemistry , biochemistry , statistics , mathematics , gene
A peptidomimetic compound undergoes a reversible single‐crystal‐to‐single‐crystal transformation upon guest release/uptake with the transformation involving a drastic conformational change. The extensive and reversible alteration in the solid state is connected to the formation of an unprecedented “CH–π zipper” which can reversibly open and close (through the formation of CH–π interactions), thus allowing for guest sensing.