Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 531513
Title Templated co-assembly into nanorods of polyanions and artificial virus capsid proteins
Author(s) Hernandez-Garcia, A.; Cohen Stuart, M.A.; Vries, R. De
Source Soft Matter 14 (2017)1. - ISSN 1744-683X - p. 132 - 139.
DOI https://doi.org/10.1039/c7sm02012k
Department(s) Physical Chemistry and Soft Matter
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2017
Abstract Recombinant triblock polypeptides C-Sn-B, where C is a 400 amino acid long hydrophilic random coil block, Sn is a multimer of the silk-like octapeptide S = (GAGAGAGQ), and B = K12 is an oligolysine, have previously been shown to encapsulate double stranded DNA into rod-shaped, virus-like particles. In order to gain insight of the co-assembly process, and in order to be able to use these proteins for templating other types of nanorods, we here explore their co-assembly with a range of polyanionic templates: poly(acrylic acids) (PAA) of a wide range of lengths, poly(styrene sulphonate) (PSS) and the stiff anionic polysaccharide xanthan. The formation of the complexes was characterized using Dynamic Light Scattering (DLS), cryogenic Transmission Electronic Microscopy (Cryo-TEM) and Atomic Force Microscopy (AFM). Except at very high molar masses, we find that flexible anionic PAA and PSS lead to co-assembly of proteins with single polyanion chains into nanorods, with a packing factor as expected on the basis of charge stochiometry. Only for very long PAA templates (8 × 105 Da) we find evidence for heterogeneous complexes with thin and thick sections. For the very stiff xanthan chains, we find that its stiffness precludes co-assembly with the artificial viral capsid proteins into condensed and regular nanorods. Given the simple and robust formation of rod-like structures with a range of polyanionic templates, we anticipate that the artificial virus proteins will be useful for preparing high-aspect ratio nanoparticles and scaffolds of precise size and find applications in nanotechnology and materials science for which currently natural rod-like viruses are being explored.
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