Metal ion-induced self-assembly and packaging of CCMV nanocapsules

Lise Schoonen, Mark B. van Eldijk, Jan C.M. van Hest

Research output: Chapter in Book/Report/Conference proceedingChapterAcademicpeer-review

1 Citation (Scopus)

Abstract

The controlled self-assembly of protein cages is vital for the use of these nanocompartments in biomedical and nanotechnological applications. Recently, we showed that by combining different structural peptide elements, it is possible to assemble viral capsid proteins in distinct well-defined morphologies. In this chapter, a triblock copolypeptide is discussed, consisting of a metal ion-coordinating hexahistidine tag, a stimulus-responsive elastin-like polypeptide and a pH-responsive self-assembling viral capsid protein. This protein is able to form two different types of capsids, depending on the assembly pathway that is followed. Here, we focus on the metal ion-induced assembly process and describe the relevant experimental procedures to induce and utilize this assembly behavior.

Original languageEnglish
Title of host publicationProtein scaffolds
Subtitle of host publicationdesign, synthesis, and applications
EditorsA.K. Udit
Place of PublicationDordrecht
PublisherSpringer
Pages57-67
Number of pages11
ISBN (Electronic)978-1-4939-7893-9
ISBN (Print)978-1-4939-7892-2
DOIs
Publication statusPublished - 5 Jun 2018

Publication series

NameMethods in Molecular Biology
Volume1798
ISSN (Print)1064-3745

Keywords

  • Affinity chromatography
  • Cowpea chlorotic mottle virus
  • Elastin-like polypeptide
  • Hexahistidine
  • His-tag
  • Metal ion
  • Self-assembly
  • Viral capsid
  • Metals/chemistry
  • Models, Molecular
  • Virion/ultrastructure
  • Virus Assembly
  • Capsid Proteins/chemistry
  • Nanocapsules/chemistry
  • Bromovirus/physiology
  • Capsid/chemistry
  • Protein Conformation
  • Recombinant Fusion Proteins/chemistry
  • Spectrum Analysis
  • Ions/chemistry

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