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

Peltzer, Raphael Mathias; Kolli, Hima Bindu; Stocker, Achim; Cascella, Michele (2018). Self-Assembly of α-Tocopherol Transfer Protein Nanoparticles: A Patchy Protein Model. The Journal of Physical Chemistry B, 122(28), pp. 7066-7072. American Chemical Society 10.1021/acs.jpcb.8b05936

Full text not available from this repository. (Request a copy)

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.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Departement of Chemistry and Biochemistry

UniBE Contributor:

Stocker, Achim

Subjects:

500 Science > 570 Life sciences; biology
500 Science > 540 Chemistry

ISSN:

1520-5207

Publisher:

American Chemical Society

Language:

English

Submitter:

Anja Ebeling

Date Deposited:

11 Mar 2020 15:21

Last Modified:

11 Mar 2020 15:21

Publisher DOI:

10.1021/acs.jpcb.8b05936

PubMed ID:

29944374

URI:

https://boris.unibe.ch/id/eprint/141794

Actions (login required)

Edit item Edit item
Provide Feedback