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Published on: October 4, 2011
Self-Assembly of α-Tocopherol Transfer Protein Nanoparticles: A Patchy Protein Model
Raphael Mathias Peltzer1, Hima Bindu Kolli1, Achim Stocker2
1Department of Chemistry, and Hylleraas Centre for Quantum Molecular Sciences , University of Oslo , P.O. Box 1033, Blindern, 0315 Oslo , Norway.
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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