de Santis, E; Castelletto, V; Ryadnov, M G (2015) Interfacial zippering-up of coiled-coil protein filaments. Phys. Chem. Chem. Phys., 17 (46). pp. 31055-31060.

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Abstract

Protein self-assembled materials find increasing use in medicine and nanotechnology. A challenge remains in our ability to tailor such materials at a given length scale. Here we report a de novo self-assembly topology which enables the engineering of filamentous protein nanostructures under morphological control. The rationale is exemplified by a ubiquitous self-assembly motif - an ¿-helical coiled-coil stagger. The stagger incorporates regularly spaced interfacial tryptophan residues, which allows it to zipper up into discrete filaments that bundle together without thickening by maturation. Using a combination of spectroscopy, microscopy, X-ray small-angle scattering and fibre diffraction methods we show that the precise positioning of tryptophan residues at the primary and secondary structure levels defines the extent of coiled-coil packing in resultant filaments. Applicable to other self-assembling systems, the rationale holds promise for the construction of advanced protein-based architectures and materials.

Item Type:	Article
Subjects:	Biotechnology Biotechnology > Bio-Diagnostics
Identification number/DOI:	10.1039/c5cp05938k
Last Modified:	02 Feb 2018 13:13
URI:	https://eprintspublications.npl.co.uk/id/eprint/6923