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

M. Brasch; Jeroen Johannes Lambertus Maria Cornelissen

doi:10.1039/C1CC13185K

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

M. Brasch, Jeroen Johannes Lambertus Maria Cornelissen

Research output: Contribution to journal › Article › Academic › peer-review

14 Citations (Scopus)

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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.

Original language	Undefined
Pages (from-to)	1446-1448
Number of pages	2
Journal	Chemical communications
Volume	48
Issue number	10
DOIs	https://doi.org/10.1039/C1CC13185K
Publication status	Published - 2012

Keywords

IR-85022
METIS-293512

Access to Document

10.1039/C1CC13185K

Cite this

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title = "Relative size selection of a conjugated polyelectrolyte in virus-like protein structures",

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.",

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AU - Cornelissen, Jeroen Johannes Lambertus Maria

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AB - 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.

KW - IR-85022

KW - METIS-293512

U2 - 10.1039/C1CC13185K

DO - 10.1039/C1CC13185K

M3 - Article

SN - 1359-7345

VL - 48

SP - 1446

EP - 1448

JO - Chemical communications

JF - Chemical communications

IS - 10

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