Potential dependent change in local structure of ferrocenyl-terminated molecular islands by electrochemical frequency modulation atomic force microscopy

2010 ◽  
Vol 28 (3) ◽  
pp. C4D40-C4D45 ◽  
Author(s):  
Ken-ichi Umeda ◽  
Ken-ichi Fukui
Keyword(s):  
Atomic Force Microscopy ◽  
Frequency Modulation ◽  
Local Structure ◽  
Force Microscopy ◽  
Atomic Force ◽  
Dependent Change ◽  
Molecular Islands

scholarly journals Resolving Structure and Mechanical Properties at the Nanoscale of Viruses with Frequency Modulation Atomic Force Microscopy

PLoS ONE ◽  
2012 ◽  
Vol 7 (1) ◽  
pp. e30204 ◽  
Author(s):  
David Martinez-Martin ◽  
Carolina Carrasco ◽  
Mercedes Hernando-Perez ◽  
Pedro J. de Pablo ◽  
Julio Gomez-Herrero ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Atomic Force Microscopy ◽  
Frequency Modulation ◽  
Force Microscopy ◽  
Atomic Force

Mapping and imaging for rapid atom discrimination: A study of frequency modulation atomic force microscopy

2009 ◽  
Vol 94 (2) ◽  
pp. 023108 ◽  
Author(s):  
Yoshiaki Sugimoto ◽  
Takashi Namikawa ◽  
Masayuki Abe ◽  
Seizo Morita
Keyword(s):  
Atomic Force Microscopy ◽  
Frequency Modulation ◽  
Force Microscopy ◽  
Atomic Force

Self-assembled monolayers of sulfonate-terminated alkanethiols investigated by frequency modulation atomic force microscopy in liquid

2017 ◽  
Vol 28 (45) ◽  
pp. 455603 ◽  
Author(s):  
Hitoshi Asakawa ◽  
Natsumi Inada ◽  
Kaito Hirata ◽  
Sayaka Matsui ◽  
Takumi Igarashi ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Frequency Modulation ◽  
Self Assembled Monolayers ◽  
Force Microscopy ◽  
Atomic Force ◽  
Assembled Monolayers ◽  
Self Assembled

High-Resolution Frequency-Modulation Atomic Force Microscopy in Liquids Using Electrostatic Excitation Method

2010 ◽  
Vol 3 (6) ◽  
pp. 065205 ◽  
Author(s):  
Ken-ichi Umeda ◽  
Noriaki Oyabu ◽  
Kei Kobayashi ◽  
Yoshiki Hirata ◽  
Kazumi Matsushige ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
High Resolution ◽  
Frequency Modulation ◽  
Force Microscopy ◽  
Atomic Force ◽  
Excitation Method

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

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Lukas Stühn ◽  
Julia Auernhammer ◽  
Christian Dietz
Keyword(s):  
Atomic Force Microscopy ◽  
Ph Value ◽  
Surrounding Medium ◽  
Real Space ◽  
Iron Storage ◽  
Liquid Environment ◽  
Force Microscopy ◽  
Atomic Force ◽  
Dependent Change ◽  
Protein Shell

AbstractFerritin, 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.

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