Interfacial zippering-up of coiled-coil protein filaments.

Content Provider	Semantic Scholar
Author	Santis, Emiliana De Castelletto, Valeria Ryadnov, Maxim G.
Copyright Year	2015
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 α-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.
Starting Page	46
Ending Page	51
Page Count	6
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://pubs.rsc.org/en/content/getauthorversionpdf/C5CP05938K
PubMed reference number	26534782v1
Alternate Webpage(s)	https://doi.org/10.1039/c5cp05938k
DOI	10.1039/c5cp05938k
Journal	Physical chemistry chemical physics : PCCP
Volume Number	17
Issue Number	46
Language	English
Access Restriction	Open
Subject Keyword	Anatomy, Regional Architecture as Topic Coil Device Component Coiled-Coil Domain Nanostructured Materials Protein Domain Scattering, Small Angle Tryptophan
Content Type	Text
Resource Type	Article