Stühn, Lukas and Auernhammer, Julia and Dietz, Christian (2019):
pH-depended protein shell dis- and reassembly of ferritin nanoparticles revealed by atomic force microscopy.
In: Scientific Reports, (1), 9. Springer Nature, e-ISSN 2045-2322,
DOI: 10.25534/tuprints-00009681,
[Online-Edition: https://tuprints.ulb.tu-darmstadt.de/9681],
Secondary publishing via sponsored Golden Open Access, [Article]
Abstract
Ferritin, a protein that is present in the human body for a controlled iron storage and release, consists of a ferrihydrite core and a protein shell. Apoferritin, the empty shell of ferritin, can be modified to carry tailored properties exploitable for targeted and direct drug delivery. This protein shell has the ability to dis- and reassemble depending on the pH value of the liquid environment and can thus be filled with the desired substance. Here we observed the dis- and reassembly process of the protein shell of ferritin and apoferritin in situ and in real space using atomic force microscopy. Ferritin and apoferritin nanoparticles adsorbed on a mica substrate exhibited a change in their size by varying the pH value of the surrounding medium. Lowering the pH value of the solution led to a decrease in size of the nanoparticles whereas a successive increase of the pH value increased the particle size again. The pH dependent change in size could be related to the dis- and reassembling of the protein shell of ferritin and apoferritin. Supplementary imaging by bimodal magnetic force microscopy of ferritin molecules accomplished in air revealed a polygonal shape of the core and a three-fold symmetry of the protein shell providing valuable information about the substructure of the nanoparticles.
| Item Type: | Article |
|---|---|
| Erschienen: | 2019 |
| Creators: | Stühn, Lukas and Auernhammer, Julia and Dietz, Christian |
| Title: | pH-depended protein shell dis- and reassembly of ferritin nanoparticles revealed by atomic force microscopy |
| Language: | English |
| Abstract: | Ferritin, a protein that is present in the human body for a controlled iron storage and release, consists of a ferrihydrite core and a protein shell. Apoferritin, the empty shell of ferritin, can be modified to carry tailored properties exploitable for targeted and direct drug delivery. This protein shell has the ability to dis- and reassemble depending on the pH value of the liquid environment and can thus be filled with the desired substance. Here we observed the dis- and reassembly process of the protein shell of ferritin and apoferritin in situ and in real space using atomic force microscopy. Ferritin and apoferritin nanoparticles adsorbed on a mica substrate exhibited a change in their size by varying the pH value of the surrounding medium. Lowering the pH value of the solution led to a decrease in size of the nanoparticles whereas a successive increase of the pH value increased the particle size again. The pH dependent change in size could be related to the dis- and reassembling of the protein shell of ferritin and apoferritin. Supplementary imaging by bimodal magnetic force microscopy of ferritin molecules accomplished in air revealed a polygonal shape of the core and a three-fold symmetry of the protein shell providing valuable information about the substructure of the nanoparticles. |
| Journal or Publication Title: | Scientific Reports |
| Number: | 1 |
| Publisher: | Springer Nature |
| Divisions: | 11 Department of Materials and Earth Sciences 11 Department of Materials and Earth Sciences > Material Science 11 Department of Materials and Earth Sciences > Material Science > Physics of Surfaces |
| Date Deposited: | 15 Dec 2019 20:56 |
| DOI: | 10.25534/tuprints-00009681 |
| Official URL: | https://tuprints.ulb.tu-darmstadt.de/9681 |
| URN: | urn:nbn:de:tuda-tuprints-96816 |
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