Colloidal Crystallization of Virus-Like Particles with Polycations

12 March 2025, Version 1
This content is a preprint and has not undergone peer review at the time of posting.

Abstract

Virus-like particles (VLPs) are protein nanocages capable of encapsulating or attaching guest molecules. Unlike viruses, they do not replicate in cells, making them promising candidates for advanced biomaterial design, particularly for biomedical applications such as drug delivery. However, the mechanisms governing VLP self-assembly into highly ordered suprastructures with enhanced functionality remain largely unexplored. This study investigates the development of pH-responsive biomaterials using the icosahedral Acinetobacter phage coat protein AP205 VLP with a diameter of around 28 nm. Small-angle X-ray scattering, dynamic light scattering, and zeta-potential measurements reveal that AP205 self-assembles with the polycation poly[2-(methacryloyloxy)ethyl] trimethylammonium chloride into highly ordered suprastructures. The structural organization is strongly influenced by composition, pH, and ionic strength. The findings provide insight into the directional interactions governing VLP self-assembly, enabling the design of tunable VLP-based biomaterials.

Keywords

self-assembly
colloidal crystals
virus-like particles
protein nanocages
SAXS

Comments

Comments are not moderated before they are posted, but they can be removed by the site moderators if they are found to be in contravention of our Commenting Policy [opens in a new tab] - please read this policy before you post. Comments should be used for scholarly discussion of the content in question. You can find more information about how to use the commenting feature here [opens in a new tab] .
This site is protected by reCAPTCHA and the Google Privacy Policy [opens in a new tab] and Terms of Service [opens in a new tab] apply.