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A Protein-Based Encapsulation System with Calcium-Controlled Cargo Loading and Detachment
Lund Univ, Biochem & Struct Biol, POB 124, Lund, Sweden..
Lund Univ, Biochem & Struct Biol, POB 124, Lund, Sweden..
Univ Utrecht, Biomol Mass Spectrometry & Prote, Bijvoet Ctr Biomol Res, Padualaan 8, NL-3584 CH Utrecht, Netherlands.;Univ Utrecht, Utrecht Inst Pharmaceut Sci, Padualaan 8, NL-3584 CH Utrecht, Netherlands..
Lund Univ, Biochem & Struct Biol, POB 124, Lund, Sweden..
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2018 (English)In: Angewandte Chemie International Edition, ISSN 1433-7851, E-ISSN 1521-3773, Vol. 57, no 35, p. 11334-11338Article in journal (Refereed) Published
Abstract [en]

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 hepatitisB 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 beta-glucosidase activity.

Place, publisher, year, edition, pages
Wiley-VCH Verlagsgesellschaft, 2018. Vol. 57, no 35, p. 11334-11338
Keywords [en]
fluorescence correlation spectroscopy, hepatitis B, protein design, self-assembly, virus-like particles
National Category
Chemical Sciences
Identifiers
URN: urn:nbn:se:kth:diva-235126DOI: 10.1002/anie.201806466ISI: 000442340000038PubMedID: 29975817Scopus ID: 2-s2.0-85051084389OAI: oai:DiVA.org:kth-235126DiVA, id: diva2:1248613
Funder
The Crafoord FoundationScience for Life Laboratory - a national resource center for high-throughput molecular bioscience
Note

QC 20180917

Available from: 2018-09-17 Created: 2018-09-17 Last updated: 2018-09-17Bibliographically approved

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Wennmalm, Stefan

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