Tag: high-speed atomic force microscopy

Real-time tracking of ionic nano-domains under shear flow

The behaviour of ions at solid–liquid interfaces underpins countless phenomena, from the conduction of nervous impulses to charge transfer in solar cells. In most cases, ions do not operate as isolated entities, but in conjunction with neighbouring ions and the surrounding solution. In aqueous solutions, recent studies suggest the existence of group dynamics through water-mediated clusters but results allowing direct tracking of ionic domains with atomic precision are scarce. *

Atomic force microscopy (AFM) can image single ions adsorbed at various solid–liquid interfaces. One of the main advantages of the technique is its ability to probe individual ions in-situ but with local contextual information about the interface over tens of nanometres at the point of measurement.*

High-speed atomic force microscopy (HS-AFM) operates similarly to standard AFM but with enhanced temporal resolution and can capture images at video rate, making it possible to track many molecular processes in real-time.*

In the article “Real-time tracking of ionic nano-domains under shear flow” Clodomiro Cafolla and Kislon Voïtchovsky use high-speed atomic force microscopy to track the evolution of Rb+, K+, Na+ and Ca2+ nano-domains containing 20 to 120 ions adsorbed at the surface of mica in aqueous solution. The interface is exposed to a shear flow able to influence the lateral motion of single ions and clusters. *

They report the achievement of single-ion spatial resolution with ~ 2 s temporal resolution.*

During the measurements, the AFM cantilever and the sample were fully immersed in the aqueous ionic solution of interest. The AFM probes used were NanoWorld Arrow-UHF ultra-high frequency AFM cantilevers. *

The results presented in the article provide some quantitative insights into the relationship between single ion properties and group dynamics at the solid–liquid interface in the presence of a microscale shear flow, with potential technological applications from manufacturing biomedical devices to enhancing the performance of aqueous ion-batteries.*

Figure 1 from “Real-time tracking of ionic nano-domains under shear flow” by Clodomiro Cafolla and Kislon Voïtchovsky: Example of time evolution for adsorbed Rb+ ions at the mica-water interface in the presence of a shear flow. (a) A time-lapse sequence shows consecutive high-resolution HS-AFM topographical images of Rb+ ions at the interface between mica and a 5 mM RbCl aqueous solution. Rb+ ions appear as bright orange-yellow protrusions standing taller than the mica surface (purple-black). Periodic rows and larger domains are clearly visible as well as singly adsorbed rubidium ions. (b) Representative image analysis highlighting Rb+ ions as orange markers (obtained by thresholding) and the idealised underlying lattice derived by inverse Fourier transform of the filtered power spectrum in each image of (a) (see ESI Section 3 for details on the procedure). (c) The algorithm automatically associates neighbouring ions (within distances < 0.52 nm) to the same cluster. Domains smaller than 5 ions are discarded here. The different clusters derived in each image are highlighted using different colours, keeping for each cluster the same colour over time. The cyan-coloured cluster offers a good example of temporal evolution. The scale bars in (a–c) represent 3 nm and the z-scale in (a) corresponds to 0.8 nm. NanoWorld Arrow-UHF ultra-high speed AFM probes were used for the high-speed atomic force microscopy (HS-AFM).
Figure 1 from “Real-time tracking of ionic nano-domains under shear flow” by Clodomiro Cafolla and Kislon Voïtchovsky:
Example of time evolution for adsorbed Rb+ ions at the mica-water interface in the presence of a shear flow. (a) A time-lapse sequence shows consecutive high-resolution HS-AFM topographical images of Rb+ ions at the interface between mica and a 5 mM RbCl aqueous solution. Rb+ ions appear as bright orange-yellow protrusions standing taller than the mica surface (purple-black). Periodic rows and larger domains are clearly visible as well as singly adsorbed rubidium ions. (b) Representative image analysis highlighting Rb+ ions as orange markers (obtained by thresholding) and the idealised underlying lattice derived by inverse Fourier transform of the filtered power spectrum in each image of (a) (see ESI Section 3 for details on the procedure). (c) The algorithm automatically associates neighbouring ions (within distances < 0.52 nm) to the same cluster. Domains smaller than 5 ions are discarded here. The different clusters derived in each image are highlighted using different colours, keeping for each cluster the same colour over time. The cyan-coloured cluster offers a good example of temporal evolution. The scale bars in (a–c) represent 3 nm and the z-scale in (a) corresponds to 0.8 nm.

*Clodomiro Cafolla and Kislon Voïtchovsky
Real-time tracking of ionic nano-domains under shear flow
Nature Scientific Reports volume 11, Article number: 19540 (2021)
DOI: https://doi.org/10.1038/s41598-021-98137-y

Please follow this external link to read the full article: https://rdcu.be/cPRBu

Open Access The article “Real-time tracking of ionic nano-domains under shear flow” by Clodomiro Cafolla and Kislon Voïtchovsky is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

Adsorption of SARS-CoV-2 Spike Protein S1 at Oxide Surfaces Studied by High-Speed Atomic Force Microscopy

The ongoing coronavirus disease 2019 (COVID-19) pandemic caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) represents a serious threat to the health of millions of people. Respiratory viruses such as SARS-CoV-2 can be transmitted via airborne and fomite routes. The latter requires virion adsorption at abiotic surfaces and most likely involves the SARS-CoV-2 spike protein subunit 1 (S1), which is the outermost point of its envelope. Understanding S1 spike protein interaction with fomite surfaces thus represents an important milestone on the road to fighting the spread of COVID-19.*

In the article “Adsorption of SARS-CoV-2 Spike Protein S1 at Oxide Surfaces Studied by High-Speed Atomic Force Microscopy “ Yang Xin, Guido Grundmeier and Adrian Keller describe how high-speed atomic force microscopy (HS-AFM) is used to monitor the adsorption of the SARS-CoV-2 spike protein S1 at Al2O3(0001) and TiO2(100) surfaces in situ. *

NanoWorld Ultra-Short Cantilevers of the USC-F0.3-k0.3 AFM probe type were used for the high-speed atomic force microscopy. *

Figure 2 from Yang Xin et al Adsorption of SARS-CoV-2 Spike Protein S1 at Oxide Surfaces Studied by High-Speed Atomic Force Microscopy HS-AFM images (1 × 1 μm2) of SARS-CoV-2 spike protein S1 in 10 mM Tris (pH 7.5) adsorbed to a) an Al2O3(0001) and b) a TiO2(100) surface recorded at different time points as indicated. Height scales are 5 nm for the clean substrate surfaces at 0 s and 12 nm for the protein covered surfaces at later time points. Below the HS-AFM images, the corresponding height distribution functions are depicted. The vertical lines in the plots represent the height thresholds applied in the statistical analyses. NanoWorld Ultra-Short Cantilevers of the USC-F0.3-k0.3 AFM probe type were used for the high-speed atomic force microscopy.
Figure 2 from Yang Xin et al Adsorption of SARS-CoV-2 Spike Protein S1 at Oxide Surfaces Studied by High-Speed Atomic Force Microscopy
HS-AFM images (1 × 1 μm2) of SARS-CoV-2 spike protein S1 in 10 mM Tris (pH 7.5) adsorbed to a) an Al2O3(0001) and b) a TiO2(100) surface recorded at different time points as indicated. Height scales are 5 nm for the clean substrate surfaces at 0 s and 12 nm for the protein covered surfaces at later time points. Below the HS-AFM images, the corresponding height distribution functions are depicted. The vertical lines in the plots represent the height thresholds applied in the statistical analyses.

*Yang Xin, Guido Grundmeier, Adrian Keller
Adsorption of SARS-CoV-2 Spike Protein S1 at Oxide Surfaces Studied by High-Speed Atomic Force Microscopy
Advanced NanoBioMed Research, Volume 1, Issue 2, February 2021, 2000024
DOI: https://doi.org/10.1002/anbr.202000024

Open Access : The article “Adsorption of SARS-CoV-2 Spike Protein S1 at Oxide Surfaces Studied by High-Speed Atomic Force Microscopy” by Yang Xin, Guido Grundmeier and Adrian Keller is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit https://creativecommons.org/licenses/by/4.0/.

Actin filaments on Mica with APTES

Courtesy of Prof. Noriyuki Kodera, nanoLSI, Kanazawa University, Japan we could upload two new images and a very nice High Speed Atomic Force Microscopy (HS-AFM) video of Actin filaments on Mica with APTES to the image gallery and the video gallery on https://www.highspeedscanning.com/.

NanoWorld USC-F1.2-k0.15 Ultra-Short AFM cantilevers [C = 0.15 N/m; fo = 1200 kHz] were used for the high speed imaging.

HS-AFM Images of actin filaments on Mica with APTES. Buffer:100 mM KCl, 2 mM MgCl2, 1 mM EGTA, 20 mM Imidazole-HCl, pH7.6 (a) 250×250 nm2 and (b) 400×400 nm2. Image courtesy of Prof. Kodera, nanoLSI, Kanazawa University, Japan. NanoWorld USC-F1.2-k0.15 AFM probes from the Ultra-Short Cantilever (USC) series were used for the High Speed Atomic Force Microscopy
HS-AFM Images of actin filaments on Mica with APTES. Buffer:100 mM KCl, 2 mM MgCl2, 1 mM EGTA, 20 mM Imidazole-HCl, pH7.6 (a) 250×250 nm2 and (b) 400×400 nm2. Images courtesy of Prof. Kodera, nanoLSI, Kanazawa University, Japan. NanoWorld USC-F1.2-k0.15 AFM probes were used for the High Speed Atomic Force Microscopy

The HighSpeedScanning webpage is dedicated to presenting information about ultra high frequency AFM probe solutions for High Speed AFM ranging from already commercialized AFM probes such as the ArrowTM UHF and NanoWorld Ultra-Short Cantilever (USC) series to AFM probes that are still under development.

Additionally to the High-Speed AFM images and videos researchers worldwide kindly have provided us with so that we can share them with the whole High Speed AFM community you will also find  a list of links and references dedicated to High-Speed AFM on https://www.highspeedscanning.com/high-speed-scanning.html 

We are aware that these lists are far from complete and we are constantly working on keepting them up to date.  If your research institute or company is working with High Speed AFM (HS-AFM) using our AFM probes or if you have published articles with images that were achieved with our High Speed AFM probes annd you find that are missing from our list then please let us know via email: info@highspeedscanning.com if you would like us to add them to the list of references .