Browse
Submit Data
Databases
API
Help

Dataset Information

23 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

3D-printed cellular tips for tuning fork atomic force microscopy in shear mode.

ABSTRACT: Conventional atomic force microscopy (AFM) tips have remained largely unchanged in nanomachining processes, constituent materials, and microstructural constructions for decades, which limits the measurement performance based on force-sensing feedbacks. In order to save the scanning images from distortions due to excessive mechanical interactions in the intermittent shear-mode contact between scanning tips and sample, we propose the application of controlled microstructural architectured material to construct AFM tips by exploiting material-related energy-absorbing behavior in response to the tip-sample impact, leading to visual promotions of imaging quality. Evidenced by numerical analysis of compressive responses and practical scanning tests on various samples, the essential scanning functionality and the unique contribution of the cellular buffer layer to imaging optimization are strongly proved. This approach opens new avenues towards the specific applications of cellular solids in the energy-absorption field and sheds light on novel AFM studies based on 3D-printed tips possessing exotic properties.

SUBMITTER: Sun L

PROVIDER: S-EPMC7661501 | biostudies-literature |

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Similar Datasets

Jumping mode atomic force microscopy on grana membranes from spinach.

Project description:The thylakoid membrane system is a complex membrane system that organizes and reorganizes itself to provide plants optimal chemical energy from sunlight under different and varying environmental conditions. Grana membranes are part of this system and contain the light-driven water-splitting enzyme Photosystem II (PSII) and light-harvesting antenna complexes. Here, we present a direct visualization of PSII complexes within grana membranes from spinach. By means of jumping mode atomic force microscopy in liquid, minimal forces were applied between the scanning tip and membrane or protein, allowing complexes to be imaged with high detail. We observed four different packing arrangements of PSII complexes, which occur primarily as dimers: co-linear crystalline rows, nanometric domains of straight or skewed rows, and disordered domains. Upon storing surface-adhered membranes at low temperature prior to imaging, large-scale reorganizations of supercomplexes between PSII and light-harvesting complex II could be induced. The highest resolution images show the existence of membrane domains without obvious topography extending beyond supercomplexes. These observations illustrate the possibility for diffusion of proteins and smaller molecules within these densely packed membranes.

| S-EPMC3234741 | biostudies-literature

Dynamic nano-triboelectrification using torsional resonance mode atomic force microscopy.

Project description:Understanding the mechanism of charge generation, distribution, and transfer between surfaces is very important for energy harvesting applications based on triboelectric effect. Here, we demonstrate dynamic nanotriboelectrification with torsional resonance (TR) mode atomic force microscopy (AFM). Experiments on rubbing the sample surface using TR mode for the generation of triboelectric charges and in-situ characterization of the charge distribution using scanning Kelvin probe microcopy (SKPM) were performed. This method allows the tip to perform lateral oscillation and maintains the tip-sample interaction in the attractive region to ensure high efficiency of the charge generation during the rubbing process. The measured efficiency of generating triboelectric charges can achieve ~10.53 times higher than conventional static/contact mode in the triboelectrification experiments. In addition to the charge generation, local discharging experiments were also performed. This work would provide a new method to generate patterned charges and also be helpful in understanding the mechanism of nanotriboelectrification.

| S-EPMC4908601 | biostudies-literature

Measuring biomaterials mechanics with atomic force microscopy. 1. Influence of the loading rate and applied force (pyramidal tips).

Project description:Atomic force microscopy (AFM) is today an established tool in imaging and determination of mechanical properties of biomaterials. Due to their complex organization, those materials show intricate properties such as viscoelasticity. Therefore, one has to consider that the loading rate at which the sample is probed will lead to different mechanical response (properties). In this work, we studied the dependence of the mechanical properties of endothelial cells on the loading rate using AFM in force spectroscopy mode. We employed a sharp, four-sided pyramidal indenter and loading rates ranging from 0.5 to 20??m/s. In addition, by variation of the load (applied forces from 100 to 10,000 pN), the dependence of the cell properties on indentation depth could be determined. We then showed that the mechanical response of endothelial cells depends nonlinearly on the loading rate and follows a weak power-law. In addition, regions of different viscous response at varying indentation depth could be determined. Based on the results we obtained, a general route map for AFM users for design of cell mechanics experiments was described.

| S-EPMC6767567 | biostudies-literature

A Semi-Automated Positioning System for contact-mode Atomic Force Microscopy (AFM).

Project description:Contact mode Atomic Force Microscopy (CM-AFM) is popularly used by the biophysics community to study mechanical properties of cells cultured in petri dishes, or tissue sections fixed on microscope slides. While cells are fairly easy to locate, sampling in spatially heterogeneous tissue specimens is laborious and time-consuming at higher magnifications. Furthermore, tissue registration across multiple magnifications for AFM-based experiments is a challenging problem, suggesting the need to automate the process of AFM indentation on tissue. In this work, we have developed an image-guided micropositioning system to align the AFM probe and human breast-tissue cores in an automated manner across multiple magnifications. Our setup improves efficiency of the AFM indentation experiments considerably. Note to Practitioners: Human breast tissue is by nature heterogeneous, and in the samples we studied, epithelial tissue is formed by groups of functional breast epithelial cells that are surrounded by stromal tissue in a complex intertwined way. Therefore sampling a specific cell type on an unstained specimen is very difficult. To aid us, we use digital stained images of the same tissue annotated by a certified pathologist to identify the region of interest (ROI) at a coarse magnification and an image-guided positioning system to place the unstained tissue near the AFM probe tip. Using our setup, we could considerably reduce AFM operating time and we believe that our setup is a viable supplement to commercial AFM stages with limited X-Y range.

| S-EPMC3840952 | biostudies-literature

Localization atomic force microscopy.

Project description:Understanding structural dynamics of biomolecules at the single-molecule level is vital to advancing our knowledge of molecular mechanisms. Currently, there are few techniques that can capture dynamics at the sub-nanometre scale and in physiologically relevant conditions. Atomic force microscopy (AFM)1 has the advantage of analysing unlabelled single molecules in physiological buffer and at ambient temperature and pressure, but its resolution limits the assessment of conformational details of biomolecules2. Here we present localization AFM (LAFM), a technique developed to overcome current resolution limitations. By applying localization image reconstruction algorithms3 to peak positions in high-speed AFM and conventional AFM data, we increase the resolution beyond the limits set by the tip radius, and resolve single amino acid residues on soft protein surfaces in native and dynamic conditions. LAFM enables the calculation of high-resolution maps from either images of many molecules or many images of a single molecule acquired over time, facilitating single-molecule structural analysis. LAFM is a post-acquisition image reconstruction method that can be applied to any biomolecular AFM dataset.

| S-EPMC8697813 | biostudies-literature

Functional dependence of resonant harmonics on nanomechanical parameters in dynamic mode atomic force microscopy.

Project description:We present a combined theoretical and experimental study of the dependence of resonant higher harmonics of rectangular cantilevers of an atomic force microscope (AFM) as a function of relevant parameters such as the cantilever force constant, tip radius and free oscillation amplitude as well as the stiffness of the sample's surface. The simulations reveal a universal functional dependence of the amplitude of the 6th harmonic (in resonance with the 2nd flexural mode) on these parameters, which can be expressed in terms of a gun-shaped function. This analytical expression can be regarded as a practical tool for extracting qualitative information from AFM measurements and it can be extended to any resonant harmonics. The experiments confirm the predicted dependence in the explored 3-45 N/m force constant range and 2-345 GPa sample's stiffness range. For force constants around 25 N/m, the amplitude of the 6th harmonic exhibits the largest sensitivity for ultrasharp tips (tip radius below 10 nm) and polymers (Young's modulus below 20 GPa).

| S-EPMC5405692 | biostudies-literature

Contact-mode high-resolution high-speed atomic force microscopy movies of the purple membrane.

Project description:High-speed atomic force microscopy (HS-AFM) is becoming a reference tool for the study of dynamic biological processes. The spatial and time resolutions of HS-AFM are on the order of nanometers and milliseconds, respectively, and allow structural and functional characterization of biological processes at the single-molecule level. In this work we present contact-mode HS-AFM movies of purple membranes containing two-dimensional arrays of bacteriorhodopsin (bR). In high-resolution movies acquired at a 100 ms frame acquisition time, the substructure on individual bR trimers was visualized. In regions in between different bR arrays, dynamic topographies were observed and interpreted as motion of the bR trimers. Similarly, motion of bR monomers in the vicinity of lattice defects in the purple membrane was observed. Our findings indicate that the bR arrays are in a mobile association-dissociation equilibrium. HS-AFM on membranes provides novel perspectives for analyzing the membrane diffusion processes of nonlabeled molecules.

| S-EPMC2749746 | biostudies-literature

Electrostatic Discovery Atomic Force Microscopy.

Project description:While offering high resolution atomic and electronic structure, scanning probe microscopy techniques have found greater challenges in providing reliable electrostatic characterization on the same scale. In this work, we offer electrostatic discovery atomic force microscopy, a machine learning based method which provides immediate maps of the electrostatic potential directly from atomic force microscopy images with functionalized tips. We apply this to characterize the electrostatic properties of a variety of molecular systems and compare directly to reference simulations, demonstrating good agreement. This approach offers reliable atomic scale electrostatic maps on any system with minimal computational overhead.

| S-EPMC8793147 | biostudies-literature

Deep atomic force microscopy.

Project description:The Atomic Force Microscope (AFM) possesses several desirable imaging features including the ability to produce height profiles as well as two-dimensional images, in fluid or air, at high resolution. AFM has been used to study a vast selection of samples on the scale of angstroms to micrometers. However, current AFMs cannot access samples with vertical topography of the order of 100 μm or greater. Research efforts have produced AFM scanners capable of vertical motion greater than 100 μm, but commercially available probe tip lengths are still typically less than 10 μm high. Even the longest probe tips are below 100 μm and even at this range are problematic. In this paper, we present a method to hand-fabricate "Deep AFM" probes with tips of the order of 100 μm and longer so that AFM can be used to image samples with large scale vertical topography, such as fractured bone samples.

| S-EPMC3869821 | biostudies-other

Polynomial force approximations and multifrequency atomic force microscopy.

Project description:We present polynomial force reconstruction from experimental intermodulation atomic force microscopy (ImAFM) data. We study the tip-surface force during a slow surface approach and compare the results with amplitude-dependence force spectroscopy (ADFS). Based on polynomial force reconstruction we generate high-resolution surface-property maps of polymer blend samples. The polynomial method is described as a special example of a more general approximative force reconstruction, where the aim is to determine model parameters that best approximate the measured force spectrum. This approximative approach is not limited to spectral data, and we demonstrate how it can be adapted to a force quadrature picture.

| S-EPMC3701428 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data