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Lorenzo Di Michele

Researcher at Imperial College London

Publications -  69
Citations -  1487

Lorenzo Di Michele is an academic researcher from Imperial College London. The author has contributed to research in topics: Membrane & Chemistry. The author has an hindex of 18, co-authored 52 publications receiving 1096 citations. Previous affiliations of Lorenzo Di Michele include University of Cambridge.

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Multistep kinetic self-assembly of DNA-coated colloids

TL;DR: This work proposes strategies to direct the gelation of two-component colloidal mixtures by sequentially activating selective interactions and investigates morphological changes in the structure of the arrested phases both by means of molecular dynamics simulations and experimentally by using DNA-coated colloids.
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Arrested demixing opens route to bigels

TL;DR: A mechanism of aggregation through arrested demixing in binary colloidal mixtures, which leads to the formation of a yet unexplored class of materials––bigels, which is obtained by tuning interspecies interactions.
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Developments in understanding and controlling self assembly of DNA-functionalized colloids

TL;DR: The latest achievements in understanding and controlling DNA-mediated interactions between colloidal particles are reviewed, which are expected to solve the decennial issues encountered in the self assembly of DNA-coated colloids.
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Volume and porosity thermal regulation in lipid mesophases by coupling mobile ligands to soft membranes

TL;DR: A model providing a thorough understanding of the thermal response of pairs and networks of DNA-tethered liposomes is developed, explaining the emergent properties out of the interplay between the temperature-dependent deformability of the vesicles and the DNA-mediated adhesive forces.
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True Molecular Scale Visualization of Variable Clustering Properties of Ryanodine Receptors

TL;DR: Analysis of molecular maps showed significant variations in the co-clustering stoichiometry between junctophilin-2 and RyR, even between nearby nanodomains, constituting an additional level of complexity in RyR arrangement and regulation of calcium signaling, intrinsically built into the nanodOMains.