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Structural analysis of the foldecture derived from racemic peptide foldamers
Gong, Jintaek,Eom, Jae-Hoon,Jeong, Rokam,Driver, Russell W.,Lee, Hee-Seung Elsevier 2017 SOLID STATE SCIENCES Vol.70 No.-
<P><B>Abstract</B></P> <P>The molecular packing structure of an elongated parallelogram plate shaped foldecture composed of a 1:1 racemic mixture of 11-helical peptide foldamers was resolved by powder X-ray diffraction (PXRD) analysis. A comprehensive Rietveld refinement procedure compensated for powder texture and identified the principal face of the foldecture. Each foldamer makes head-to-tail intermolecular hydrogen bonds, creating extended chains of single enantiomers that form a network of hydrophobic close contacts with foldamers of both the opposite and the same chiralities. An isosurface for anisotropic microstrain was calculated and found to be smallest along the x-axis, which is parallel to the network of intermolecular hydrogen bonds. Comparison with the single crystal structure found molecular packing motifs to be almost identical—a result infrequently observed in enantiopure foldectures. This is the first powder X-ray diffraction structural analysis of a foldecture composed of multiple components.</P> <P><B>Highlights</B></P> <P> <UL> <LI> The first example of the molecular packing structure of foldecture composed of multiple components was reported. </LI> <LI> The anisotropic microstrain analysis showed intermolecular interactions with the direction of racemic foldamers. </LI> <LI> The formation of enantiomeric pairs was proposed in the initial nucleation stage of the self-assembly process. </LI> </UL> </P>