Month: September 2018

Boron nitride nanoresonators for phonon-enhanced molecular vibrational spectroscopy at the strong coupling limit

In the article “Boron nitride nanoresonators for phonon-enhanced molecular vibrational spectroscopy at the strong coupling limit” the authors use, for the first time, phonon-polariton-resonant h-BN ribbons for SEIRA spectroscopy of small amounts of organic molecules in Fourier transform infrared spectroscopy. They demonstrate a new way to strongly couple infrared light and molecular vibrations, by utilizing phonon polariton nanoresonators made of hexagonal boron nitride, a Van der Waals material.

For the nanoscale Fourier transform infrared (nano-FTIR) spectroscopy mentioned in this article an oscillating Pt/Ir coated NanoWorld Arrow-NCPt AFM probe was illuminated by p-polarized mid-IR broadband radiation.

Figure 2 from "Boron nitride nanoresonators for phonon-enhanced molecular vibrational spectroscopy at the strong coupling limit": Far- and near-field spectroscopic characterization of h-BN ribbon arrays. (a) Sketch of the transmission spectroscopy experiment. Incoming light at normal incidence is polarized perpendicular to the ribbons to excite the HPhP resonance. (b) Transmission spectrum normalized to the bare substrate spectrum, T/T0, for a 20 × 20 μm2 h-BN ribbon array. Ribbon width w=158 nm, ribbon period D=400 nm and ribbon height h=40 nm. (c) Sketch of the nano-FTIR spectroscopy experiment. The near-field probing tip is scanned across (y-direction) the h-BN ribbon in 20-nm steps, as indicated by the dashed blue line. Near-field spectra are recorded as a function of the tip position (the detector signal is demodulated at the third harmonic of the tip tapping frequency, yielding s3(y, ω), as explained in the Materials and methods section). (d) Lower panel: Spectral line scan s3(y, ω), where each horizontal line corresponds to a spectrum recorded at a fixed y-position (vertical axis). Upper panel: Illustration of the real part of the z-component of the electric field (Re[Ez]) profile across the ribbon at the resonance frequency observed in the nano-FTIR spectra (lower panel). The AFM tip used was a NanoWorld Arrow-NCPT
Figure 2 from “Boron nitride nanoresonators for phonon-enhanced molecular vibrational spectroscopy at the strong coupling limit”: Far- and near-field spectroscopic characterization of h-BN ribbon arrays. (a) Sketch of the transmission spectroscopy experiment. Incoming light at normal incidence is polarized perpendicular to the ribbons to excite the HPhP resonance. (b) Transmission spectrum normalized to the bare substrate spectrum, T/T0, for a 20 × 20 μm2 h-BN ribbon array. Ribbon width w=158 nm, ribbon period D=400 nm and ribbon height h=40 nm. (c) Sketch of the nano-FTIR spectroscopy experiment. The near-field probing tip is scanned across (y-direction) the h-BN ribbon in 20-nm steps, as indicated by the dashed blue line. Near-field spectra are recorded as a function of the tip position (the detector signal is demodulated at the third harmonic of the tip tapping frequency, yielding s3(y, ω), as explained in the Materials and methods section). (d) Lower panel: Spectral line scan s3(y, ω), where each horizontal line corresponds to a spectrum recorded at a fixed y-position (vertical axis). Upper panel: Illustration of the real part of the z-component of the electric field (Re[Ez]) profile across the ribbon at the resonance frequency observed in the nano-FTIR spectra (lower panel).

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

Marta Autore, Peining Li, Irene Dolado, Francisco J Alfaro-Mozaz, Ruben Esteban, Ainhoa Atxabal, Fèlix Casanova, Luis E Hueso, Pablo Alonso-González, Javier Aizpurua, Alexey Y Nikitin, Saül Vélez & Rainer Hillenbrand
Boron nitride nanoresonators for phonon-enhanced molecular vibrational spectroscopy at the strong coupling limit
Light: Science & Applications 7, 17172 (2018)
DOI: https://doi.org/10.1038/lsa.2017.172

For the full article please follow this external link: https://rdcu.be/7B0F

The article: Boron nitride nanoresonators for phonon-enhanced molecular vibrational spectroscopy at the strong coupling limit by Marta Autore et. al, is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

Vertical Light Sheet Enhanced Side-View Imaging for AFM Cell Mechanics Studies

Atomic Force Microscopy is a powerful tool for evaluating cell mechanics.
In the recent article “Vertical Light Sheet Enhanced Side-View Imaging for AFM Cell Mechanics Studies” by Kellie Beicker, E. Timothy O’Brien III, Michael R. Falvo, Richard Superfine published in Nature Scientific Reports, the authors combine sideways imaging and a vertical light sheet illumination system integrated with AFM to achieve their results.

5 µm polystyrene beads attached to NanoWorld Arrow-TL1 tipless AFM probes were used.

igure 5 from Vertical Light Sheet Enhanced Side-View Imaging for AFM Cell Mechanics Studies: Membrane and nuclear displacements observed in response to force-rupture events between the AFM-tip and cell membrane. (a) Retraction portion of force-indentation curve with important points (A-G) identified. A, the point of zero force application to the cell, B-F, force-rupture peaks, and G, after bead releases from cell. (b) A closer examination of peaks E and F with sub-peaks of the E rupture event identified. No point is shown for E1 because this is the frame immediately following Peak E0. Inset indicates regions where displacement is measured between points E and F highlighted in green. These regions were determined through difference imaging using frames taken at E and F. (c) Regions of cell displacements determined through difference imaging highlighted in green for the sub-peaks indicated in (b). Yellow dashed lines indicate outline of AFM mounted bead. Scale bars = 5 um. NanoWorld Arrow-TL1 tipless AFM cantilevers were used.
Figure 5 from Beicker et. al Vertical Light Sheet Enhanced Side-View Imaging for AFM Cell Mechanics Studies: Membrane and nuclear displacements observed in response to force-rupture events between the AFM-tip and cell membrane. (a) Retraction portion of force-indentation curve with important points (A-G) identified. A, the point of zero force application to the cell, B-F, force-rupture peaks, and G, after bead releases from cell. (b) A closer examination of peaks E and F with sub-peaks of the E rupture event identified. No point is shown for E1 because this is the frame immediately following Peak E0. Inset indicates regions where displacement is measured between points E and F highlighted in green. These regions were determined through difference imaging using frames taken at E and F. (c) Regions of cell displacements determined through difference imaging highlighted in green for the sub-peaks indicated in (b). Yellow dashed lines indicate outline of AFM mounted bead. Scale bars = 5 um.

Kellie Beicker, E. Timothy O’Brien III, Michael R. Falvo, Richard Superfine
Vertical Light Sheet Enhanced Side-View Imaging for AFM Cell Mechanics Studies
Nature Scientific Reports,  8, Article number: 1504 (2018)
DOI: https://doi.org/10.1038/s41598-018-19791-3

For the full article please follow this external link: https://rdcu.be/59FM

The article Beicker et. al, Vertical Light Sheet Enhanced Side-View Imaging for AFM Cell Mechanics Studies 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/.

 

Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins

We have a month with “R” again and the shellfish season has started in the Northern Hemisphere. So we’d like to share the Nature Communications article by Petrone et. al “Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins” with you.
A NanoWorld Pointprobe® NCSTR AFM probe was used for the AFM images in this paper. This AFM probe is designed to give extra stability and accuracy during soft tapping mode imaging in order to produce higher quality AFM images while minimizing sample damage.

Supplementary Figure 16 from Petrone et. al "Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins": Atomic Force Microscopy (AFM) of mussel adhesive proteins on mica. AFM images of dry Pvfp-3α and Pvfp-5β adsorbed from 0.02 mg ml-1 solution in 5% acetic acid and 0.25 MO3 on mica. After 20 min adsorption, the mica surfaces were washed with protein -free buffer, and the AFM images show the homogenous distribution of the resulting adsorbed proteins. The height profiles for both proteins are shown in the graphs below, corresponding to the dotted red and blue lines in the respective AFM images (see black arrows).
Supplementary Figure 16 from Petrone et. al “Mussel adhesion is dictated by time-regulated
secretion and molecular conformation of mussel adhesive proteins”:
Atomic Force Microscopy (AFM) of mussel adhesive proteins on mica. AFM images of dry Pvfp-3α and Pvfp-5β adsorbed from 0.02 mg ml-1 solution in 5% acetic acid and 0.25 MO3 on mica. After 20 min adsorption, the mica surfaces were washed with protein -free buffer, and the AFM images show the homogenous distribution of the resulting adsorbed proteins. The height profiles for both proteins are shown in the graphs below, corresponding to the dotted red and blue lines in the respective AFM images (see black arrows).

Luigi Petrone, Akshita Kumar, Clarinda N. Sutanto, Navinkumar J. Patil, Srinivasaraghavan Kannan, Alagappan Palaniappan, Shahrouz Amini, Bruno Zappone, Chandra Verma, Ali Miserez
Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins
Nature Communications volume 6, Article number: 8737 (2015)
DOI https://doi.org/10.1038/ncomms9737

Please follow this external link for the full article: https://rdcu.be/5vcI

The article by Petrone, L.et al. “Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins” is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/