Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 135, Issue 41, Pages 15565-15578Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja4074529
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Funding
- NSF [CHE-1012620, 0923395, CHE-0131013]
- Division of Chemical Sciences, Geosciences, and Biosciences, Office of Basic Energy Sciences of the U.S. Department of Energy [DE-ER15377]
- Emory University, Children's Healthcare of Atlanta
- Center for AIDS Research at Emory University [P30 AI050409]
- Georgia Research Alliance
- US DOE Office of Basic Energy Sciences, Division of Material Sciences [W-31-109-Eng-38]
- Direct For Biological Sciences
- Div Of Biological Infrastructure [0923395] Funding Source: National Science Foundation
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1012620] Funding Source: National Science Foundation
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Design of a structurally defined helical assembly is described that involves recoding of the amino acid sequence of peptide GCN4-pAA. In solution and the crystalline state, GCN4-pAA adopts a 7-helix bundle structure that resembles a supramolecular lock washer. Structurally informed mutagenesis of the sequence of GCN4-pAA afforded peptide 7HSAP1, which undergoes self-association into a nanotube via noncovalent interactions between complementary interfaces of the coiled-coil lock-washer structures. Biophysical measurements conducted in solution and the solid state over multiple length scales of structural hierarchy are consistent with self-assembly of nanotube structures derived from 7-helix bundle subunits. The dimensions of the supramolecular assemblies are similar to those observed in the crystal structure of GCN4-pAA. Fluorescence studies of the interaction of 7HSAP1 with the solvatochromic fluorophore PRODAN indicated that the nanotubes could encapsulate shape-appropriate small molecules with high binding affinity.
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