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Folding Patterns in a Family of Oligoamide Foldamers
Author(s) -
Kortelainen Minna,
Suhonen Aku,
Hamza Andrea,
Pápai Imre,
Nauha Elisa,
YliniemeläSipari Sanna,
Nissinen Maija,
Pihko Petri M.
Publication year - 2015
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201406521
Subject(s) - foldamer , conformational isomerism , chemistry , folding (dsp implementation) , intramolecular force , crystallography , protein folding , hydrogen bond , aryl , stereochemistry , computational chemistry , molecule , biochemistry , alkyl , organic chemistry , electrical engineering , engineering
Abstract A series of small, unsymmetrical pyridine‐2,6‐dicarboxylamide oligoamide foldamers with varying lengths and substituents at the end groups were synthetized to study their conformational properties and folding patterns. The @‐type folding pattern resembled the oxyanion‐hole motifs of enzymes, but several alternative folding patterns could also be characterized. Computational studies revealed several alternative conformers of nearly equal stability. These folding patterns differed from each other in their intramolecular hydrogen‐bonding patterns and aryl–aryl interactions. In the solid state, the foldamers adopted either the globular @‐type fold or the more extended S‐type conformers, which were very similar to those foldamers obtained computationally. In some cases, the same foldamer molecule could even crystallize into two different folding patterns, thus confirming that the different folding patterns are very close in energy in spite of their completely different shapes. Finally, the best match for the observed NOE interactions in the liquid state was a conformation that matched the computationally characterized helix‐type fold.