Tag: atomic force microscopy

A Short Peptide Hydrogel with High Stiffness Induced by 310‐Helices to β‐Sheet Transition in Water

In the article “A Short Peptide Hydrogel with High Stiffness Induced by 310‐Helices to β‐Sheet Transition in Water” by Shu Hui Hiew, Harini Mohanram, Lulu Ning, Jingjing Guo, Antoni Sánchez‐Ferrer, Xiangyan Shi, Konstantin Pervushin, Yuguang Mu, Raffaele Mezzenga and Ali Miserez, a short biomimetic peptide composed of eight amino acid residues derived from squid sucker ring teeth proteins is demonstrated to form hydrogel in water without any cross‐linking agent or chemical modification and exhibits a stiffness on par with the stiffest peptide hydrogels.
Their study broadens the range of secondary structures available to create supramolecular hydrogels, and introduces 310‐helices as transient building blocks for gelation via a 310‐to‐β‐sheet conformational transition.*

The AFM images presented in this study were obtained in soft tapping mode using NanoWorld Pointprobe® NCSTR AFM probes.

Figure 1 from «A Short Peptide Hydrogel with High Stiffness Induced by
310‐ Helices to β‐Sheet Transition in Water” by Shu Hui Hiew et al.
Structural features and physico‐chemical properties of GV8 peptide hydrogel observed with time‐series spectroscopy measurements during gelation
b) AFM amplitude profile of dried GV8 hydrogel with fibers of ≈6–10 nm height.

*Shu Hui Hiew, Harini Mohanram, Lulu Ning, Jingjing Guo, Antoni Sánchez‐Ferrer, Xiangyan Shi, Konstantin Pervushin, Yuguang Mu, Raffaele Mezzenga, Ali Miserez
A Short Peptide Hydrogel with High Stiffness Induced by 310‐Helices to β‐Sheet Transition in Water
Advanced Science 2019, 1901173
Doi: https://doi.org/10.1002/advs.201901173

Please follow this external link to read the full article: https://onlinelibrary.wiley.com/doi/full/10.1002/advs.201901173

Open Access: The article « A Short Peptide Hydrogel with High Stiffness Induced by 310‐Helices to β‐Sheet Transition in Water » ” by Shu Hui Hiew, Harini Mohanram, Lulu Ning, Jingjing Guo, Antoni Sánchez‐Ferrer, Xiangyan Shi, Konstantin Pervushin, Yuguang Mu, Raffaele Mezzenga and Ali Miserez 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 thirdparty 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/.

    Simultaneous Quantification of the Interplay Between Molecular Turnover and Cell Mechanics by AFM–FRAP

    Quantifying the adaptive mechanical behavior of living cells is essential for the understanding of their inner working and function.*

    In their article “Simultaneous Quantification of the Interplay Between Molecular Turnover and Cell Mechanics by AFM–FRAP” Mark Skamrahl, Huw Colin‐York, Liliana Barbieri and Marco Fritzsche use a combination of atomic force microscopy and fluorescence recovery after photobleaching is introduced which offers simultaneous quantification and direct correlation of molecule kinetics and mechanics in living cells.*

    Simultaneous quantification of the relationship between molecule kinetics and cell mechanics may thus open up unprecedented insights into adaptive mechanobiological mechanisms of cells.*

    For the AFM nanoindentation tests described in their publication the authors used NanoWorld Arrow-TL2 tipless cantilevers that were functionalized with a polystyrene bead with 5 µm radius.*

    Figure 1 a from “Simultaneous Quantification of the Interplay Between Molecular Turnover and Cell Mechanics by AFM–FRAP” by M. Skamrahl et al.: Establishment and calibration of the optomechanical AFM–FRAP platform. a) Schematic of the AFM–FRAP setup illustrating the experimental power of simultaneous quantification of molecule kinetics and cell mechanics
    Figure 1 a from “Simultaneous Quantification of the Interplay Between Molecular Turnover and Cell Mechanics by AFM–FRAP” by M. Skamrahl et al.:
    Establishment and calibration of the optomechanical AFM–FRAP platform. a) Schematic of the AFM–FRAP setup illustrating the experimental power of simultaneous quantification of molecule kinetics and cell mechanics

    *Mark Skamrahl, Huw Colin‐York, Liliana Barbieri, Marco Fritzsche
    Simultaneous Quantification of the Interplay Between Molecular Turnover and Cell Mechanics by AFM–FRAP
    Small 2019, 1902202
    DOI: https://doi.org/10.1002/smll.201902202

    Please follow this external link to the full article https://onlinelibrary.wiley.com/doi/full/10.1002/smll.201902202

    Open Access: The article « Simultaneous Quantification of the Interplay Between Molecular Turnover and Cell Mechanics by AFM–FRAP » by Mark Skamrahl, Huw Colin‐York, Liliana Barbieri and Marco Fritzsche 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 thirdparty 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/.