Structural analysis of the foldecture derived from racemic peptide foldamers

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 identicalda result infrequently observed in enantiopure foldectures. This is the first powder Xray diffraction structural analysis of a foldecture composed of multiple components. (C) 2017 Elsevier Masson SAS. All rights reserved.
Publisher
ELSEVIER SCIENCE BV
Issue Date
2017-08
Language
English
Keywords

X-RAY STRUCTURES; MOLECULAR ARCHITECTURES; TRANS-2-AMINOCYCLOPENTANECARBOXYLIC ACID; PROTEIN CRYSTALLOGRAPHY; ALPHA/BETA-PEPTIDES; CHEMICAL-SYNTHESIS; CRYSTAL-STRUCTURES; DIMERIZATION; FULLERIDE; DESIGN

Citation

SOLID STATE SCIENCES, v.70, pp.1 - 5

ISSN
1293-2558
DOI
10.1016/j.solidstatesciences.2017.05.014
URI
http://hdl.handle.net/10203/225200
Appears in Collection
CH-Journal Papers(저널논문)
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