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Biology subjects

Elbourne, A.

Publications and source records attributed to Elbourne, A..

2 recordsLinked to original sources

Real-time Biomechanical Characterisation of Cytoskeletal Remodelling

As progenitors for tissue, human mesenchymal stem cells (hMSCs) with ability of self-proliferation and differentiation into various cell types such as osteocytes and adipocytes show great potential applications for tissue engineering. Stem cell fate regulation is highly affected by the cytoskeleton structure and mechanical properties. In this paper, quantitative Atomic Force Microscopy (Q-AFM) was used to continuously characterise topography and biomechanical properties while applying cytoskeleton disruptors to hMSCs. The cell stiffness (quantified by Youngs modulus), primarily governed by the cytoskeleton network, had quantifiable changes associated with cytoskeleton polymerisation and depolymerisation when treatments were applied. Furthermore, with Q-AFM measurements, these changes were tracked in real time over a period of minutes to hours, and the biomechanical properties of the cells were tracked through the applied treatment and subsequent recovery post treatment. Here we present the capability of Q-AFM to perform real time biomechanical characterisation of living cells, directly correlated to intracellular structure and cytoskeletal remodelling.

biophysics↗

Exploring the Self-Assembly of Encapsulin Protein Nanocages from Different Structural Classes

Encapsulins, self-assembling icosahedral protein nanocages derived from prokaryotes, represent a versatile set of tools for nanobiotechnology. However, a comprehensive understanding of the mechanisms underlying encapsulin self-assembly, disassembly, and reassembly is lacking. Here, we characterise the disassembly/reassembly properties of three encapsulin nanocages that possess different structural architectures: T = 1 (24 nm), T = 3 (32 nm), and T = 4 (42 nm). Using spectroscopic techniques and electron microscopy, encapsulin architectures were found to exhibit varying sensitivities to the denaturant guanidine hydrochloride (GuHCl), extreme pH, and elevated temperature. While all encapsulins showed the capacity to reassemble following GuHCl-induced disassembly (within 75 min), only the smallest T = 1 nanocage reassembled after disassembly in basic pH (within 15 min). Furthermore, atomic force microscopy revealed that all encapsulins showed a significant loss of structural integrity after undergoing sequential disassembly/reassembly steps. These findings provide insights into encapsulins disassembly/reassembly dynamics, thus informing their future design, modification, and application.

biophysics↗