Optical monitoring of in situ iron loading into single, native ferritin proteins

Yousefi, A. ORCID: 0000-0001-7478-7991, Ying, C. ORCID: 0000-0002-7279-1388, Parmenter, C.D.J., Assadipapari, M., Sanderson, G., Zheng, Z. ORCID: 0000-0002-9676-2856, Xu, L. ORCID: 0000-0001-9071-4311, Zargarbashi, S., Hickman, G.J. ORCID: 0000-0002-4632-9229, Cousins, R.B., Mellor, C.J., Mayer, M. and Rahmani, M. ORCID: 0000-0001-9268-4793, 2023. Optical monitoring of in situ iron loading into single, native ferritin proteins. Nano Letters, 23 (8), pp. 3251-3258. ISSN 1530-6984

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Abstract

Ferritin is a protein that stores and releases iron to prevent diseases associated with iron dysregulation in plants, animals, and bacteria. The conversion between iron-loaded holo-ferritin and empty apo-ferritin is an important process for iron regulation. To date, studies of ferritin have used either ensemble measurements to quantify the characteristics of a large number of proteins or single-molecule approaches to interrogate labeled or modified proteins. Here we demonstrate the first real-time study of the dynamics of iron ion loading and biomineralization within a single, unlabeled ferritin protein. Using optical nanotweezers, we trapped single apo- and holo-ferritins indefinitely, distinguished one from the other, and monitored their structural dynamics in real time. The study presented here deepens the understanding of the iron uptake mechanism of ferritin proteins, which may lead to new therapeutics for iron-related diseases.

Item Type: Journal article
Publication Title: Nano Letters
Creators: Yousefi, A., Ying, C., Parmenter, C.D.J., Assadipapari, M., Sanderson, G., Zheng, Z., Xu, L., Zargarbashi, S., Hickman, G.J., Cousins, R.B., Mellor, C.J., Mayer, M. and Rahmani, M.
Publisher: American Chemical Society (ACS)
Date: 26 April 2023
Volume: 23
Number: 8
ISSN: 1530-6984
Identifiers:
NumberType
10.1021/acs.nanolett.3c00042DOI
1755642Other
Rights: Copyright © 2023 The Authors. Published by American Chemical Society. Open access using a Creative Commons Attribution licence 4.0 International (CC BY 4.0).
Divisions: Schools > School of Science and Technology
Record created by: Linda Sullivan
Date Added: 10 May 2023 09:42
Last Modified: 10 May 2023 09:42
URI: https://irep.ntu.ac.uk/id/eprint/48914

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