Protein Cage Nanoparticles for Hybrid Inorganic–Organic Materials

Qazi, Shefah; Lucon, Janice; Uchida, Masaki; Douglas, Trevor

doi:10.1002/9781118571811.ch11

Cited by 2 publications

(3 citation statements)

References 159 publications

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“…Finally, the Prot-QDs are able to enter into living cells, showing great cell labeling capacity at very low doses without affecting cell viability, making them useful tools for biomedical applications. In addition, the approach developed in this work could be translated into other protein cage architectures (presenting α-helices structures), that have been previously used as templates for the synthesis of different nanomaterials, − to tune the properties of the resulting protein–hybrid nanomaterial for their application in different fields.…”

Section: Discussionmentioning

confidence: 99%

Protein Design for the Synthesis and Stabilization of Highly Fluorescent Quantum Dots

2020

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Quantum dots (QDs) are studied intensively nowadays as fluorescent probes for biomedical applications due to their high emission quantum yield, excellent resistance to photo-bleaching, photo-stability and large Stokes shift, when contrasted with commonly utilized organic fluorescent dyes. This study introduces a protein engineering approach to incorporate metal coordination sites for the sustainable synthesis and stabilization of biocompatible CdS QDs in proteins. The resulting protein-stabilized CdS QDs (Prot-QDs), generated by a green aqueous route at 37 ºC, are highly photo-luminescent and photo-stable, have a long shelf-life and high stability under physiological conditions. The Prot-QDs showed effective internalization and high fluorescence in cells, even at low doses, and biocompatibility. This work focuses on CdS QDs, since this composition has been extensively studied, however this approach could be easily translated to QDs with other metal composition. Here, protein design emerges as promising approach to generate protein-nanomaterial hybrids as broadly applicable tools in different applications such as light-emitting devices, metal ion detection, and biomedical applications.

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Section: Discussionmentioning

confidence: 99%

Protein Design for the Synthesis and Stabilization of Highly Fluorescent Quantum Dots

2020

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“…[ 9 ] Molecular crowded environments within the cell are mimicked in molecular ensembles using artificial crowding agents, [ 10 ] for example, PEG, Ficoll, and triton, that can induce undesired effects, such as aggregation or binding. [ 11 , 12 ] In this context, the development of nanoscale molecular containers [ 13 – 15 ] imitates the fundamental biological problems regarding compartmentalization [ 16 , 17 ] with promising technological applications. [ 18 ] Encapsulation protects molecules from harsh environments [ 19 ] and in contrast to systems of free molecules, [ 10 ] the packing fraction determines the cargo microenvironment, thus minimizing the influence of external factors.…”

Section: Introductionmentioning

confidence: 99%

“…[ 24 ] Truncated SP interacts with CP by an helix-loop-helix motif [ 25 ] so that non-native cargo molecules can be genetically fused to either of the N- or C-termini. [ 15 , 26 ] By contrast to infectious phages, these engineered VLPs have 12 identical pentons with no portal [ 27 ] resulting in a higher symmetrical structure that enables a homogeneous distribution of the cargo. Leveraging the P22 VLP self-assembly mechanism and the role of SP, a variety of proteinaceous cargo molecules have successfully been encapsulated using both in vivo and in vitro approaches, with the latter affording compositional control of the encapsulated cargo.…”

Section: Introductionmentioning

confidence: 99%

Electromechanical Photophysics of GFP Packed Inside Viral Protein Cages Probed by Force‐Fluorescence Hybrid Single‐Molecule Microscopy

Strobl

Selivanovitch

Ibáñez‐Freire

et al. 2022

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Packing biomolecules inside virus capsids has opened new avenues for the study of molecular function in confined environments. These systems not only mimic the highly crowded conditions in nature, but also allow their manipulation at the nanoscale for technological applications. Here, green fluorescent proteins are packed in virus‐like particles derived from P22 bacteriophage procapsids. The authors explore individual virus cages to monitor their emission signal with total internal reflection fluorescence microscopy while simultaneously changing the microenvironment with the stylus of atomic force microscopy. The mechanical and electronic quenching can be decoupled by ≈10% each using insulator and conductive tips, respectively. While with conductive tips the fluorescence quenches and recovers regardless of the structural integrity of the capsid, with the insulator tips quenching only occurs if the green fluorescent proteins remain organized inside the capsid. The electronic quenching is associated with the coupling of the protein fluorescence emission with the tip surface plasmon resonance. In turn, the mechanical quenching is a consequence of the unfolding of the aggregated proteins during the mechanical disruption of the capsid.

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Protein Cage Nanoparticles for Hybrid Inorganic–Organic Materials

Cited by 2 publications

References 159 publications

Protein Design for the Synthesis and Stabilization of Highly Fluorescent Quantum Dots

Protein Design for the Synthesis and Stabilization of Highly Fluorescent Quantum Dots

Electromechanical Photophysics of GFP Packed Inside Viral Protein Cages Probed by Force‐Fluorescence Hybrid Single‐Molecule Microscopy

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