Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

A Protein-Based Encapsulation System with Calcium-Controlled Cargo Loading and Detachment

Lizatović, Robert ; Assent, Marvin ; Barendregt, Arjan ; Dahlin, Jonathan ; Bille, Anna LU ; Satzinger, Katharina LU ; Tupina, Dagnija ; Heck, Albert J.R. ; Wennmalm, Stefan and André, Ingemar LU orcid (2018) In Angewandte Chemie - International Edition 57(35). p.11334-11338
Abstract

Protein-based encapsulation systems have a wide spectrum of applications in targeted delivery of cargo molecules and for chemical transformations in confined spaces. By engineering affinity between cargo and container proteins it has been possible to enable the efficient and specific encapsulation of target molecules. Missing in current approaches is the ability to turn off the interaction after encapsulation to enable the cargo to freely diffuse in the lumen of the container. Separation between cargo and container is desirable in drug delivery applications and in the use of capsids as catalytic nanoparticles. We describe an encapsulation system based on the hepatitis B virus capsid in which an engineered high-affinity interaction... (More)

Protein-based encapsulation systems have a wide spectrum of applications in targeted delivery of cargo molecules and for chemical transformations in confined spaces. By engineering affinity between cargo and container proteins it has been possible to enable the efficient and specific encapsulation of target molecules. Missing in current approaches is the ability to turn off the interaction after encapsulation to enable the cargo to freely diffuse in the lumen of the container. Separation between cargo and container is desirable in drug delivery applications and in the use of capsids as catalytic nanoparticles. We describe an encapsulation system based on the hepatitis B virus capsid in which an engineered high-affinity interaction between cargo and capsid proteins can be modulated by Ca2+. Cargo proteins are loaded into capsids in the presence of Ca2+, while ligand removal triggers unbinding inside the container. We observe that confinement leads to hindered rotation of cargo inside the capsid. Application of the designed container for catalysis was also demonstrated by encapsulation of an enzyme with β-glucosidase activity.

(Less)
Please use this url to cite or link to this publication:
author
; ; ; ; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
fluorescence correlation spectroscopy, hepatitis B, protein design, self-assembly, virus-like particles
in
Angewandte Chemie - International Edition
volume
57
issue
35
pages
5 pages
publisher
John Wiley & Sons Inc.
external identifiers
  • pmid:29975817
  • scopus:85051084389
ISSN
1433-7851
DOI
10.1002/anie.201806466
language
English
LU publication?
yes
id
8c781ab6-6374-4b24-bc8a-b359101b8241
date added to LUP
2018-09-13 11:15:41
date last changed
2024-02-14 01:43:49
@article{8c781ab6-6374-4b24-bc8a-b359101b8241,
  abstract     = {{<p>Protein-based encapsulation systems have a wide spectrum of applications in targeted delivery of cargo molecules and for chemical transformations in confined spaces. By engineering affinity between cargo and container proteins it has been possible to enable the efficient and specific encapsulation of target molecules. Missing in current approaches is the ability to turn off the interaction after encapsulation to enable the cargo to freely diffuse in the lumen of the container. Separation between cargo and container is desirable in drug delivery applications and in the use of capsids as catalytic nanoparticles. We describe an encapsulation system based on the hepatitis B virus capsid in which an engineered high-affinity interaction between cargo and capsid proteins can be modulated by Ca<sup>2+</sup>. Cargo proteins are loaded into capsids in the presence of Ca<sup>2+</sup>, while ligand removal triggers unbinding inside the container. We observe that confinement leads to hindered rotation of cargo inside the capsid. Application of the designed container for catalysis was also demonstrated by encapsulation of an enzyme with β-glucosidase activity.</p>}},
  author       = {{Lizatović, Robert and Assent, Marvin and Barendregt, Arjan and Dahlin, Jonathan and Bille, Anna and Satzinger, Katharina and Tupina, Dagnija and Heck, Albert J.R. and Wennmalm, Stefan and André, Ingemar}},
  issn         = {{1433-7851}},
  keywords     = {{fluorescence correlation spectroscopy; hepatitis B; protein design; self-assembly; virus-like particles}},
  language     = {{eng}},
  month        = {{08}},
  number       = {{35}},
  pages        = {{11334--11338}},
  publisher    = {{John Wiley & Sons Inc.}},
  series       = {{Angewandte Chemie - International Edition}},
  title        = {{A Protein-Based Encapsulation System with Calcium-Controlled Cargo Loading and Detachment}},
  url          = {{http://dx.doi.org/10.1002/anie.201806466}},
  doi          = {{10.1002/anie.201806466}},
  volume       = {{57}},
  year         = {{2018}},
}