Templated co-assembly into nanorods of polyanions and artificial virus capsid proteins

Recombinant triblock polypeptides C-S n -B, where C is a 400 amino acid long hydrophilic random coil block, S n is a multimer of the silk-like octapeptide S = (GAGAGAGQ), and B = K 12 is an oligolysine, have previously been shown to encapsulate double stranded DNA into rod-shaped, virus-like particl...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Soft matter 2017-12, Vol.14 (1), p.132-139
Hauptverfasser: Hernandez-Garcia, A, Cohen Stuart, M. A, de Vries, R
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung:Recombinant triblock polypeptides C-S n -B, where C is a 400 amino acid long hydrophilic random coil block, S n is a multimer of the silk-like octapeptide S = (GAGAGAGQ), and B = K 12 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 × 10 5 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. A broad range of polyanions was used to template nanorods by co-assembly with a designed recombinant artificial viral coat protein.
ISSN:1744-683X
1744-6848
DOI:10.1039/c7sm02012k