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Prof. Dr. Bernard Piette

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Department of Mathematical Sciences, University of Durham, Durham DH13LE, UK
Interests: mathematical modelling of biologocial and molecular systems

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Dear Colleagues,

Recently, a number of artificial proteins nanoparticles/cages have been created experimentally, with one of the main aims being the creation of virus-like capsids that can be used for targeted drug delivery. Proteins are assembling together to form a polygon-like shape and these so-called faces then bind together to form a polyhedron structure, which can include holes. Unlike virus cages, some of these artificial cages exhibit unexpected/paradoxical geometries that have near regular symmetry.

One open question is what are the possible geometries for those cages? What are the best polygon structures to form such cages? How thick or how tapered must the faces be to bind together into a cage-like structure? How do the buffers in which these cages are created affect the structures that are obtained? How stables are these nano-cages? How does one bind cargo inside the nanoparticles.

We are expecting both experimental and theoretical papers that help answer these questions.

Prof. Dr. Bernard Piette
Guest Editor

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Keywords

protein cages
nano cages
nanoparticles
capsid
virus
Euclidean geometry
symmetry
finite groups
planar graphs

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Research

15 pages, 3831 KiB

Open AccessArticle

Protein/Protein and Quantum Dot/Protein Organization in Sequential Monolayer Materials Studied Using Resonance Energy Transfer

by Jakub Sławski, Katarzyna Walczewska-Szewc and Joanna Grzyb

Appl. Sci. 2023, 13(21), 11917; https://doi.org/10.3390/app132111917 - 31 Oct 2023

Viewed by 674

Abstract

Controlled junctions of proteins and nanomaterials offer multiple potential applications in the further construction of nanobiodevices. One of the possible junction types is a set of sequential monolayers of various components deposited on a given substrate. The advantage of such an organization is its high sensitivity, resulting from a huge surface covered by molecules or particles. What is more, the molecules/particles adsorbed on a substrate might be easier to handle than the assay in a cuvette. For further application, there should be crosstalk between monolayers; this is defined by the type of individuals forming a complex system. Here, we are studying, using mainly confocal microscopy and FLIM imaging, crosstalk through resonance energy transfer. The sequential monolayers of fluorescent proteins and CdTe quantum dots were deposited on a convenient substrate, a polyvinylidene difluoride membrane. First, we found that the degree of coverage is lower in the second monolayer. Hence, by manipulating the order of deposition, we obtained a system with a varied yield of resonance energy transfer with a donor excess or an acceptor excess. For a deeper understanding of the energy transfer and its limitations in this system influencing the assay pursuit, we utilized Monte Carlo computation. We found that, indeed, the distance between the monolayers, as well as the degree of coverage, is crucial. With the results of the simulation, we might estimate the relative degree of coverage in our sequential monolayers. We also found that in quantum-dots/protein-composed systems, the yield is stronger than predicted by Monte Carlo simulation. Hence, there should be protein reorientation on the nanoparticle surface, leading to such an effect. Finally, we showed that the yield of resonance energy transfer may be modulated by the external application of poly-L-lysines. These chemicals influenced QD fluorescence but not protein fluorescence and might be used, therefore, as a trigger or a switch in nanobiodevices employing those types of sequential monolayers. Full article

(This article belongs to the Special Issue Design and Applications of Artificial Biomolecule Assemblies)

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