uu.seUppsala University Publications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Atomistic Simulation of Protein Encapsulation in Metal-Organic Frameworks
Beijing Univ Chem Technol, Coll Life Sci & Technol, Beijing Key Lab Bioproc, Box 53, Beijing 100029, Peoples R China.;Univ Sci & Technol Beijing, Sch Chem & Biol Engn, Dept Biol Sci & Engn, Beijing 100083, Peoples R China..
Beijing Univ Chem Technol, Coll Life Sci & Technol, Beijing Key Lab Bioproc, Box 53, Beijing 100029, Peoples R China..
Beijing Univ Chem Technol, Coll Life Sci & Technol, Beijing Key Lab Bioproc, Box 53, Beijing 100029, Peoples R China..
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
2016 (English)In: Journal of Physical Chemistry B, ISSN 1520-6106, E-ISSN 1520-5207, Vol. 120, no 3, 477-484 p.Article in journal (Refereed) Published
Resource type
Text
Abstract [en]

Fabrication of metal organic frameworks (MOFs) with large apertures triggers a brand-new research area for selective encapsulation of biomolecules within MOF nanopores. The underlying inclusion mechanism is yet to be clarified however. Here we report a molecular dynamics study on the mechanism of protein encapsulation in MOFs. Evaluation for the binding of amino acid side chain analogues reveals that van der Waals interaction is the main driving force for the binding and that-guest size acts as a key factor predicting protein binding with MOFs. Analysis on the conformation and-thermodynamic stability of the miniprotein Trp-cage encapsulated in a series of with varying pore apertures and-surface chemistries indicates,that protein encapsulation can be achieved Vial maintaining a polar/nonpolar balance in the MOF surface through tunable modification of organic linkers and Mg-O chelating moieties. Such modifications endow MOFs with a more biocompatible confinement. This work provides guidelines for selective inclusion of biomolecules within MOFs and facilitates MOF functions as a new class of host materials and molecular chaperones.

Place, publisher, year, edition, pages
2016. Vol. 120, no 3, 477-484 p.
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-278005DOI: 10.1021/acs.jpcb.5b10437ISI: 000369116000011PubMedID: 26730607OAI: oai:DiVA.org:uu-278005DiVA: diva2:906053
Available from: 2016-02-23 Created: 2016-02-23 Last updated: 2017-11-30Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed

Authority records BETA

van der Spoel, David

Search in DiVA

By author/editor
van der Spoel, David
By organisation
Department of Cell and Molecular Biology
In the same journal
Journal of Physical Chemistry B
Biochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 486 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf