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Interfacial zippering-up of coiled-coil protein filaments

DOI: 10.1039/C5CP05938K DOI Help

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