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J Am Chem Soc. 2013 Oct 16;135(41):15565-78. doi: 10.1021/ja4074529. Epub 2013 Oct 3.

Rational design of helical nanotubes from self-assembly of coiled-coil lock washers.

Author information

1
Department of Chemistry, Emory University , 1515 Dickey Drive, Atlanta, Georgia 30322, United States.

Abstract

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.

PMID:
24028069
DOI:
10.1021/ja4074529
[Indexed for MEDLINE]

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