Supramolecular virus-like particles by co-assembly of triblock polypolypeptide and PAMAM dendrimers. Issue 19 (30th April 2021)

• Record Type: Journal Article
• Authors: Zhou, Wenjuan; Liu, Lei; Huang, Jianan; Cai, Ying; Cohen Stuart, Martien A.; de Vries, Renko; Wang, Junyou
• Is Part Of: Soft matter. Volume 17:Issue 19(2021)
• Page Start: 5044
• Page End: 5049
• Publication Date: 2021-04-30
• Subjects: Soft condensed matter -- Periodicals; 530.413
• DOI: 10.1039/d1sm00290b
• Languages: English
• ISSNs: 1744-683X

Abstract

Abstract : This study reports a new assembly system based on a triblock polypolypeptide C4 -S10 -B K12 and –COONa terminated PAMAM dendrimers. The formed virus-like nanorods display well-defined structure and size, which is from the branched structure and generation-dependent size of PAMAM dendrimers. Abstract : Virus-like particles are of special interest as functional delivery vehicles in a variety of fields ranging from nanomedicine to materials science. Controlled formation of virus-like particles relies on manipulating the assembly of the viral coat proteins. Herein, we report a new assembly system based on a triblock polypolypeptide C4 -S10 -B K12 and –COONa terminated PAMAM dendrimers. The polypolypeptide has a cationic B K12 block with 12 lysines; its binding with anionic PAMAM triggers the folding of the peptide's middle silk-like block and leads to formation of virus-like nanorods, stabilized against aggregation by the long hydrophilic "C" block of the polypeptide. Varying the dendrimer/polypeptide mixing ratio hardly influences the structure and size of the nanorod. However, increasing the dendrimer generation, that is, increasing the dendrimer size results in increased particle length and height, without affecting the width of the nanorod. The branched structure and well-defined size of the dendrimers allows delicate control of the particle size; it is impossible to achieve similar control over assembly of the polypeptide with linear polyelectrolyte as template. In conclusion, we report a novel protein assembling system with properties resembling a viral coat; the findings may therefore be helpful for designing functional virus-like particles like vaccines.