Stühn, Lukas ; Auernhammer, Julia ; Dietz, Christian (2019)
pH-depended protein shell dis- and reassembly of ferritin nanoparticles revealed by atomic force microscopy.
In: Scientific Reports, 2019, 9 (1)
doi: 10.25534/tuprints-00009681
Artikel, Zweitveröffentlichung, Verlagsversion
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Kurzbeschreibung (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.
Typ des Eintrags: | Artikel |
---|---|
Erschienen: | 2019 |
Autor(en): | Stühn, Lukas ; Auernhammer, Julia ; Dietz, Christian |
Art des Eintrags: | Zweitveröffentlichung |
Titel: | pH-depended protein shell dis- and reassembly of ferritin nanoparticles revealed by atomic force microscopy |
Sprache: | Englisch |
Publikationsjahr: | 2019 |
Publikationsdatum der Erstveröffentlichung: | 2019 |
Verlag: | Springer Nature |
Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Scientific Reports |
Jahrgang/Volume einer Zeitschrift: | 9 |
(Heft-)Nummer: | 1 |
DOI: | 10.25534/tuprints-00009681 |
URL / URN: | https://tuprints.ulb.tu-darmstadt.de/9681 |
Zugehörige Links: | |
Herkunft: | Zweitveröffentlichung aus gefördertem Golden Open Access |
Kurzbeschreibung (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. |
Status: | Verlagsversion |
URN: | urn:nbn:de:tuda-tuprints-96816 |
Sachgruppe der Dewey Dezimalklassifikatin (DDC): | 600 Technik, Medizin, angewandte Wissenschaften > 600 Technik |
Fachbereich(e)/-gebiet(e): | 11 Fachbereich Material- und Geowissenschaften 11 Fachbereich Material- und Geowissenschaften > Materialwissenschaft 11 Fachbereich Material- und Geowissenschaften > Materialwissenschaft > Fachgebiet Physics of Surfaces |
Hinterlegungsdatum: | 15 Dez 2019 20:56 |
Letzte Änderung: | 15 Dez 2019 20:56 |
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