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pH-depended protein shell dis- and reassembly of ferritin nanoparticles revealed by atomic force microscopy

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

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
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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.

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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