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Self-Assembly of α-Tocopherol Transfer Protein Nanoparticles: A Patchy Protein Model

Type of publication Peer-reviewed
Publikationsform Original article (peer-reviewed)
Author Peltzer Raphael Mathias, Kolli Hima Bindu, Stocker Achim, Cascella Michele,
Project The role of CRALBP in the chemistry of vision
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Original article (peer-reviewed)

Journal The Journal of Physical Chemistry B
Volume (Issue) 122(28)
Page(s) 7066 - 7072
Title of proceedings The Journal of Physical Chemistry B
DOI 10.1021/acs.jpcb.8b05936

Open Access

URL https://doi.org/10.1021%2Facs.jpcb.8b05936
Type of Open Access Website

Abstract

We describe the mechanism of self-aggregation of α-tocopherol transfer protein into a spherical nanocage employing Monte Carlo simulations. The protein is modeled by a patchy coarse-grained representation, where the protein–protein interfaces, determined in the past by X-ray diffraction, are represented by simplified two-body interaction potentials. Our results show that the oligomerization kinetics proceeds in two steps, with the formation of metastable trimeric units and the subsequent assembly into the spherical aggregates. Data are in agreement with experimental observations regarding the prevalence of different aggregation states at specific ambient conditions. Finally, our results indicate a route for the experimental stabilization of the trimer, crucial for the understanding of the physiological role of such aggregates in vitamin E body trafficking.
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