Publication
Article Metrics
Citations
Online attention
Interfacial zippering-up of coiled-coil protein filaments
Authors:
Emiliana De
Santis
(National Physical Laboratory)
,
Valeria
Castelletto
(National Physical Laboratory)
,
Maxim G.
Ryadnov
(National Physical Laboratory)
Co-authored by industrial partner:
No
Type:
Journal Paper
Journal:
Physical Chemistry Chemical Physics
, VOL 17
, PAGES 31055 - 31060
State:
Published (Approved)
Published:
October 2015
Diamond Proposal Number(s):
11048
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 a-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 extentof 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 material
Subject Areas:
Chemistry
Instruments:
I19-Small Molecule Single Crystal Diffraction
Other Facilities: ESRF