Our distributor NanoAndMore USA has a booth @Materials_MRS MRS Fall Meeting & Exhibit 2021 in Boston this week. Visit them at booth no. 609 and find out more about NANOSENSORS AFM probes.

Electrical manipulation of skyrmions attracts considerable attention for its rich physics and promising applications. To date, such a manipulation is realized mainly via spin-polarized current based on spin-transfer torque or spin–orbital torque effect.*

However, this scheme is energy consuming and may produce massive Joule heating. To reduce energy dissipation and risk of heightened temperatures of skyrmion-based devices, an effective solution is to use electric field instead of current as stimulus.*

In the article “Electric-field-driven non-volatile multi-state switching of individual skyrmions in a multiferroic heterostructure”, Yadong Wang, Lei Wang, Jing Xia, Zhengxun Lai, Guo Tian, Xichao Zhang, Zhipeng Hou, Xingsen Gao, Wenbo Mi, Chun Feng, Min Zeng, Guofu Zhou, Guanghua Yu, Guangheng Wu, Yan Zhou, Wenhong Wang, Xi-xiang Zhang and Junming Liu realize an electric-field manipulation of skyrmions in a nanostructured ferromagnetic/ferroelectrical heterostructure at room temperature via an inverse magneto-mechanical effect.*

Intriguingly, such a manipulation is non-volatile and exhibits a multistate feature. Numerical simulations indicate that the electric-field manipulation of skyrmions originates from strain-mediated modification of effective magnetic anisotropy and Dzyaloshinskii–Moriya interaction.*

The results presented in the article open a direction for constructing low-energy-dissipation, non-volatile, and multistate skyrmion-based spintronic devices.*

To minimize the influence of the magnetic field from the MFM tip on the magnetic domain structure during the magnetic force microscopy ( MFM ) measurements, NANOSENSORS™ PPP-LM-MFMR low moment magnetic AFM probes were used.*

These MFM probes are designed for magnetic force microscopy with reduced disturbance of the magnetic sample by the tip and enhanced lateral resolution compared to the standard PPP-MFMR probe. The distance between the tip and sample was maintained at a constant distance of 30 nm.*

*Yadong Wang, Lei Wang, Jing Xia, Zhengxun Lai, Guo Tian, Xichao Zhang, Zhipeng Hou, Xingsen Gao, Wenbo Mi, Chun Feng, Min Zeng, Guofu Zhou, Guanghua Yu, Guangheng Wu, Yan Zhou, Wenhong Wang, Xi-xiang Zhang and Junming Liu
Electric-field-driven non-volatile multi-state switching of individual skyrmions in a multiferroic heterostructure
Nature Communications volume 11, Article no. 3577 (2020)
DOI: https://doi.org/10.1038/s41467-020-17354-7

Please follow this external link to read the full article: https://rdcu.be/b6qpr

Open Access: The article “Electric-field-driven non-volatile multi-state switching of individual skyrmions in a multiferroic heterostructure” by Yadong Wang, Lei Wang, Jing Xia, Zhengxun Lai, Guo Tian, Xichao Zhang, Zhipeng Hou, Xingsen Gao, Wenbo Mi, Chun Feng, Min Zeng, Guofu Zhou, Guanghua Yu, Guangheng Wu, Yan Zhou, Wenhong Wang, Xi-xiang Zhang and Junming Liu 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/.

MeCP2 and MBD2 are members of a family of proteins that possess a domain that selectively binds 5-methylcytosine in a CpG context. Members of the family interact with other proteins to modulate DNA packing. Stretching of DNA–protein complexes in nanofluidic channels with a cross-section of a few persistence lengths allows us to probe the degree of compaction by proteins.*

In the article “DNA looping by two 5-methylcytosine-binding proteins quantified using nanofluidic devices” Ming Liu, Saeid Movahed, Saroj Dangi, Hai Pan, Parminder Kaur, Stephanie M. Bilinovich, Edgar M. Faison, Gage O. Leighton, Hong Wang, David C. Williams Jr. and Robert Riehn demonstrate DNA compaction by MeCP2 while MBD2 does not affect DNA configuration. By using atomic force microscopy (AFM), they determined that the mechanism for compaction by MeCP2 is the formation of bridges between distant DNA stretches and the formation of loops.*

Despite sharing a similar specific DNA-binding domain, the impact of full-length 5-methylcytosine-binding proteins can vary drastically between strong compaction of DNA and no discernible large-scale impact of protein binding. The authors of the article demonstrate that ATTO 565-labeled MBD2 is a good candidate as a staining agent for epigenetic mapping.*

For atomic force microscopy (AFM), the authors used a 7,163-bp linear DNA substrate which contains a 1,697-bp methylated CpG-rich region that is flanked by 2,742-bp and 2,724-bp CpG-free regions. For MeCP2, the DNA substrate and the protein were diluted in AFM imaging buffer (HEPES 20 mM, Mg(OAc)210mM, NaCl 100mM, pH 7.5), mixed together and deposited on freshly peeled mica. For MBD2FLsc, the authors describe how they first mixed the protein and DNA and then diluted the sample in AFM buffer before deposition. The final MeCP2 concentration deposited on mica was 7.5nM, and the MBD2FLsc concentration was 14nM. The mica samples were then washed with filtered deionized water and dried with nitrogen.*

NANOSENSORS™ PointProbe® Plus PPP-FMR AFM probes ( ≈2.8N/m) were used to image the sample at a scan resolution of 5.9nm and a scan rate of 3μm/s.*

*Ming Liu, Saeid Movahed, Saroj Dangi, Hai Pan, Parminder Kaur, Stephanie M. Bilinovich, Edgar M. Faison, Gage O. Leighton, Hong Wang, David C. Williams Jr. and Robert Riehn
DNA looping by two 5-methylcytosine-binding proteins quantified using nanofluidic devices
Epigenetics & Chromatin volume 13, Article number: 18 (2020)
DOI: https://doi.org/10.1186/s13072-020-00339-7

Please follow this external link to read the full article: https://rdcu.be/b3iTm

Open Access: The article “DNA looping by two 5-methylcytosine-binding proteins quantified using nanofluidic devices” by Ming Liu, Saeid Movahed, Saroj Dangi, Hai Pan, Parminder Kaur, Stephanie M. Bilinovich, Edgar M. Faison, Gage O. Leighton, Hong Wang, David C. Williams Jr. and Robert Riehn 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/.