Journal
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
Volume 11, Issue 10, Pages 4147-4155Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpclett.0c00997
Keywords
-
Categories
Funding
- Qilu Young Scholarship Funding of Shandong University
- National Natural Science Foundation of China [21872087, 21901145]
- Natural Science Foundation of Jiangsu Province [BK20190209]
- Youth Cross-Scientific Innovation Group of Shandong University [2020QNQT003]
Ask authors/readers for more resources
Helical structures are important features of many important biomacromolecules such as double helices and single alpha-helices in DNA and protein, respectively, yet the self-organization of short oligopeptides (<3) or independent amino acids into artificial helical structures on the atomic level remains mysterious. Here we present the direct construction of artificial double and single helices from N-terminated aryl amino acids (ferrocene phenylalanine (Phe) conjugates) despite both Phe and Phe-Phe dipeptide self-aggregations adopting supramolecular beta-sheet structures, which also demonstrated chirality evolution exposed to small molecular binders. In the solid state, the box-shaped building unit stacks into a double helix with enantiomer-resolved handedness driven orthogonally by H-bonds and the CH-pi interaction. The entire double helix is noncovalently linked except for the hybridization regions. Asymmetric H-bonds between carboxylic acids and amides facilitates the one-dimensional helical packing of amino acid residues. The ditopic building unit adopts intramolecular H-bonds, facilitating single-strand helix formation. In aqueous self-assemblies, the superhelical structures were retained, which underwent chirality transfer and handedness inversion upon complexation orthogonally by H-bonds and charge-transfer interaction, showing adaptivity to environmental factors.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available