Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 498449
Title Orthogonal Functionalization of Ferritin via Supramolecular Re-Assembly
Author(s) Spa, Silvia J.; Bunschoten, Anton; Rood, Marcus T.M.; Peters, R.J.B.; Koster, Abraham J.; Leeuwen, F.W.B. Van
Source European Journal of Inorganic Chemistry 2015 (2015)27. - ISSN 1434-1948 - p. 4603 - 4610.
DOI https://doi.org/10.1002/ejic.201500386
Department(s) BioNanoTechnology
RIKILT - Business unit Contaminants & Toxins
Publication type Refereed Article in a scientific journal
Publication year 2015
Keyword(s) Ferritin - Insertion - Iron - Nanoparticles - Self-assembly - Supramolecular chemistry
Abstract

To investigate if the degree of functionalization of ferritin could be controlled using a supramolecular self-assembly process, two photophysical separable batches of ferritin were created by functionalizing ferritin capsids with either Cy3- or Cy5-dye (loading rate of about 50 %). After dis-assembly, Cy3-, Cy5- as well as non-functionalized ferritin subunits were mixed in variable ratios. Photophysical measurements revealed that the ratio in which the subunits were mixed was indeed indicative for the ratios in which the functionalized subunits were observed in the re-assembled capsids. During re-assembly, however, a slight preference for the inclusion of non-functionalized subunits was observed, indicating the reactivity decreased following functionalization. The iron biomineralization properties of ferritin were retained by the multi-functionalized capsids as FeII diffused rapidly inside making it visible by transmission electron microscopy (TEM). These combined data indicate that it is possible to functionalize ferritin in an orthogonal manner using the supramolecular interaction between ferritin subunits.

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