Folding Patterns in a Family of Oligoamide Foldamers |
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Authors: | Minna Kortelainen Aku Suhonen Dr Andrea Hamza Dr Imre Pápai Dr Elisa Nauha Dr Sanna Yliniemelä‐Sipari Prof Dr Maija Nissinen Prof Dr Petri M Pihko |
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Institution: | 1. Department of Chemistry, Nanoscience Center, University of Jyv?skyl?, P.O. Box 35, 40014 JYU (Finland), Fax: (+358)?14‐260‐2501;2. Institute of Organic Chemistry, Research Center for Natural Sciences, Hungarian Academy of Sciences, Magyar Tudósok K?rútja 2, 1117, Budapest (Hungary) |
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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. |
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Keywords: | crystal growth foldamers protein folding hydrogen bonds oligomerization |
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