Relative size selection of a conjugated polyelectrolyte in virus-like protein structures

Melanie Brasch; Jeroen J L M Cornelissen

doi:10.1039/c1cc13185k

Relative size selection of a conjugated polyelectrolyte in virus-like protein structures

Chem Commun (Camb). 2012 Feb 1;48(10):1446-8. doi: 10.1039/c1cc13185k. Epub 2011 Nov 28.

Authors

Melanie Brasch¹, Jeroen J L M Cornelissen

Affiliation

¹ Laboratory for Biomolecular Nanotechnology, MESA+ Institute, University of Twente, PO Box 207, 7500 AE Enschede, The Netherlands.

PMID: 22121498
DOI: 10.1039/c1cc13185k

Abstract

A conjugated polyelectrolyte poly[(2-methoxy-5-propyloxy sulfonate)-phenyl-ene vinylene] (MPS-PPV) drives the assembly of virus capsid proteins to form single virus-like particles (VLPs) and aggregates with more than two VLPs, with a relative selection of high molecular weight polymer in the latter.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Capsid Proteins / chemistry*
Electrolytes / chemistry
Molecular Weight
Particle Size
Polymers / chemistry*
Protein Conformation

Substances

Capsid Proteins
Electrolytes
Polymers