scholarly journals High speed atomic force microscopy to investigate the interactions between toxic Aβ1-42 peptides and model membranes in real time: impact of the membrane composition

Nanoscale ◽  
2019 ◽  
Vol 11 (15) ◽  
pp. 7229-7238 ◽  
Author(s):  
M. Ewald ◽  
S. Henry ◽  
E. Lambert ◽  
C. Feuillie ◽  
C. Bobo ◽  
...  

For investigating Alzheimer's disease mechanisms, high-speed atomic force microscopy is a proper tool to monitor the interactions between toxic peptides and lipid model membranes.

2017 ◽  
Vol 53 (98) ◽  
pp. 13172-13175 ◽  
Author(s):  
Keito Koizumi ◽  
Masaaki Akamatsu ◽  
Kenichi Sakai ◽  
Shinya Sasaki ◽  
Hideki Sakai

A solubilization-induced morphological change in surfactant surface aggregates was imaged in real-time, using high-speed atomic force microscopy.


2017 ◽  
Vol 8 (1) ◽  
Author(s):  
Mikihiro Shibata ◽  
Hiroshi Nishimasu ◽  
Noriyuki Kodera ◽  
Seiichi Hirano ◽  
Toshio Ando ◽  
...  

ACS Omega ◽  
2017 ◽  
Vol 2 (1) ◽  
pp. 181-185 ◽  
Author(s):  
Kazunori Ushimaru ◽  
Shoji Mizuno ◽  
Ayako Honya ◽  
Hideki Abe ◽  
Takeharu Tsuge

2020 ◽  
Vol 21 (12) ◽  
pp. 4287
Author(s):  
Takahiro Watanabe-Nakayama ◽  
Bikash R. Sahoo ◽  
Ayyalusamy Ramamoorthy ◽  
Kenjiro Ono

Individual Alzheimer’s disease (AD) patients have been shown to have structurally distinct amyloid-β (Aβ) aggregates, including fibrils, in their brain. These findings suggest the possibility of a relationship between AD progression and Aβ fibril structures. Thus, the characterization of the structural dynamics of Aβ could aid the development of novel therapeutic strategies and diagnosis. Protein structure and dynamics have typically been studied separately. Most of the commonly used biophysical approaches are limited in providing substantial details regarding the combination of both structure and dynamics. On the other hand, high-speed atomic force microscopy (HS-AFM), which simultaneously visualizes an individual protein structure and its dynamics in liquid in real time, can uniquely link the structure and the kinetic details, and it can also unveil novel insights. Although amyloidogenic proteins generate heterogeneously aggregated species, including transient unstable states during the aggregation process, HS-AFM elucidated the structural dynamics of individual aggregates in real time in liquid without purification and isolation. Here, we review and discuss the HS-AFM imaging of amyloid aggregation and strategies to optimize the experiments showing findings from Aβ and amylin, which is associated with type II diabetes, shares some common biological features with Aβ, and is reported to be involved in AD.


2012 ◽  
Vol 516 ◽  
pp. 396-401
Author(s):  
Itsuhachi Ishisaki ◽  
Yuya Ohashi ◽  
Tatsuo Ushiki ◽  
Futoshi Iwata

We developed a real-time nanomanipulation system based on high-speed atomic force microscopy (HS-AFM). During manipulation, the operation of the manipulation is momentarily interrupted for a very short time for high-speed imaging; thus, the topographical image of the fabricated surface is periodically updated during the manipulation. By using a high-speed imaging technique, the interrupting time could be much reduced during the manipulation; as a result, the operator almost does not notice the blink time of the interruption for imaging during the manipulation. As for the high-speed imaging technique, we employed a contact-mode HS-AFM to obtain topographic information through the instantaneous deflection of the cantilever during high-speed scanning. By using a share motion PZT scanner, the surface could be imaged with a frame rate of several fps. Furthermore, the high-speed AFM was coupled with a haptic device for human interfacing. By using the system, the operator can move the AFM probe into any position on the surface and feel the response from the surface during manipulation. As a demonstration of the system, nanofabrication under real-time monitoring was performed. This system would be very useful for real-time nanomanipulation and fabrication of sample surfaces.


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