Molecular Engineering of E. coli Bacterioferritin: A Versatile Nanodimensional Protein Cage

Molecules · 11 authors, 1 centre

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The work validates Bfr as a versatile platform for bionanotechnological applications such as bioimaging and materials synthesis.

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The study's central goal was to develop new strategies for controlled guest molecule encapsulation, moving beyond random entrapment. Both strategies were successful, with encapsulation confirmed by techniques like size-exclusion chromatography, fluorescence spectroscopy, and transmission electron microscopy. The implications are for advancing the design of protein-based nanocontainers for materials science and speculative future biomedical applications like drug delivery.

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other

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biomedical research

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ORIGINAL PAPER

PMC10301331

Molecular Engineering of E. coli Bacterioferritin: A Versatile Nanodimensional Protein Cage

Molecules

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ABSTRACT

Abstract Currently, intense interest is focused on the discovery and application of new multisubunit cage proteins and spherical virus capsids to the fields of bionanotechnology, drug delivery, and diagnostic imaging as their internal cavities can serve as hosts for fluorophores or bioactive molecular cargo. Bacterioferritin is unusual in the ferritin protein superfamily of iron-storage cage proteins in that it contains twelve heme cofactors and is homomeric. The goal of the present study is to expand the capabilities of ferritins by developing new approaches to molecular cargo encapsulation employing bacterioferritin. Two strategies were explored to control the encapsulation of a diverse range of molecular guests compared to random entrapment, a predominant strategy employed in this area. The first was the inclusion of histidine-tag peptide fusion sequences within the internal cavity of bacterioferritin. This approach allowed for the successful and controlled encapsulation of a fluorescent dye, a protein (fluorescently labeled streptavidin), or a 5 nm gold nanoparticle. The second strategy, termed the heme-dependent cassette strategy, involved the substitution of the native heme with heme analogs attached to (i) fluorescent dyes or (ii) nickel-nitrilotriacetate (NTA) groups (which allowed for controllable encapsulation of a histidine-tagged green fluorescent protein). An in silico docking approach identified several small molecules able to replace the heme and capable of controlling the quaternary structure of the protein. A transglutaminase-based chemoenzymatic approach to surface modification of this cage protein was also accomplished, allowing for future nanoparticle targeting. This research presents novel strategies to control a diverse set of molecular encapsulations and adds a further level of sophistication to internal protein cavity engineering. Keywords: bacterioferritin, encapsulation, bioconjugation, heme, gold, green fluorescent protein, surface modification, host–guest, transglutaminase, in silico docking

CITATION EXPORT

Anton M van der Ven, Hawa Gyamfi, Uthaiwan Suttisansanee et al.. Molecular Engineering of E. coli Bacterioferritin: A Versatile Nanodimensional Protein Cage. Molecules. (2023). https://doi.org/10.3390/molecules28124663

AUTHORS

11 · 1 CENTRES

Anton M van der Ven, Hawa Gyamfi, Uthaiwan Suttisansanee, Muhammad S Ahmad, Zhengding Su, Robert M Taylor, Amanda Poole, Sorina Chiorean, Elisabeth Daub, Taylor Urquhart, John F Honek

1Department of Chemistry, University of Waterloo, Waterloo, ON N2L 3G1, Canada; [email protected] (A.M.v.d.V.); [email protected] (H.G.); [email protected] (U.S.); [email protected] (M.S.A.); [email protected] (Z.S.); [email protected] (R.M.T.); [email protected] (A.P.); [email protected] (S.C.); [email protected] (E.D.); [email protected] (T.U.)