title: Interfacial zippering-up of coiled-coil protein filaments.
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.
authors.affiliation: National Physical Laboratory, Hampton Rd, Teddington, Middlesex, TW11 0LW, UK. max.ryadnov@npl.co.uk.
authors.forename: Emiliana De
authors.initials: ED
authors.lastname: Santis
authors.affiliation: National Physical Laboratory, Hampton Rd, Teddington, Middlesex, TW11 0LW, UK. max.ryadnov@npl.co.uk.
authors.forename: Valeria
authors.initials: V
authors.lastname: Castelletto
authors.affiliation: National Physical Laboratory, Hampton Rd, Teddington, Middlesex, TW11 0LW, UK. max.ryadnov@npl.co.uk.
authors.forename: Maxim G
authors.initials: MG
authors.lastname: Ryadnov
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D053838:Scattering, Small Angle; D017550:Spectroscopy, Fourier Transform Infrared; D014961:X-Ray Diffraction
chemical_list: D010455:Peptides