scholarly journals Development of hydrogel-based MEMS piezoresistive sensors for detection of solution pH and glucose concentration

2012 ◽  
Vol 34 (4) ◽  
pp. 281-288
Author(s):  
Trinh Quang Thong ◽  
Margarita Guenther ◽  
Gerald Gerlach

Hydrogels are water-swollen polymeric materials that maintain a distinct three-dimensional structure. Manipulation of hydrogel structure has produced stimuli sensitive hydrogels, which change their swelling degree or undergo phase transition in response to minimal changes in environmental conditions. This paper presents the development of hydrogel-based sensors for measurement of solution pH and glucose concentration using commercial MEMS piezoresistive pressure transducers. pH-sensitive PVA/PAA and glucose-sensitive AAm/3-APB/BIS hydrogels are used in the experiments. Two types of sensor packaging, one is used as solution container and the other used to dip into solution have been performed. The measurements for different solutions having pH values between 1 to 11 and glucose concentrations between 2.5 mM and 15 mM have been carried out. The output characteristics of sensors have been demonstrated showing the long-term reproduction and relatively good sensitivity, namely approximately 20 mV/pH for pH sensor and 7 mV/1 mM of glucose concentration for glucose sensor.

2019 ◽  
Vol 9 (3) ◽  
pp. 553 ◽  
Author(s):  
Monireh Bakhshpour ◽  
Neslihan Idil ◽  
Işık Perçin ◽  
Adil Denizli

The application of interconnected supermacroporous cryogels as support matrices for the purification, separation and immobilization of whole cells and different biological macromolecules has been well reported in literature. Cryogels have advantages over traditional gel carriers in the field of biochromatography and related biomedical applications. These matrices nearly mimic the three-dimensional structure of native tissue extracellular matrix. In addition, mechanical, osmotic and chemical stability of cryogels make them attractive polymeric materials for the construction of scaffolds in tissue engineering applications and in vitro cell culture, separation materials for many different processes such as immobilization of biomolecules, capturing of target molecules, and controlled drug delivery. The low mass transfer resistance of cryogel matrices makes them useful in chromatographic applications with the immobilization of different affinity ligands to these materials. Cryogels have been introduced as gel matrices prepared using partially frozen monomer or polymer solutions at temperature below zero. These materials can be produced with different shapes and are of interest in the therapeutic area. This review highlights the recent advances in cryogelation technologies by emphasizing their biomedical applications to supply an overview of their rising stars day to day.


2020 ◽  
Vol 117 (41) ◽  
pp. 25352-25359
Author(s):  
Haicheng Yao ◽  
Weidong Yang ◽  
Wen Cheng ◽  
Yu Jun Tan ◽  
Hian Hian See ◽  
...  

Electronic skins are essential for real-time health monitoring and tactile perception in robots. Although the use of soft elastomers and microstructures have improved the sensitivity and pressure-sensing range of tactile sensors, the intrinsic viscoelasticity of soft polymeric materials remains a long-standing challenge resulting in cyclic hysteresis. This causes sensor data variations between contact events that negatively impact the accuracy and reliability. Here, we introduce the Tactile Resistive Annularly Cracked E-Skin (TRACE) sensor to address the inherent trade-off between sensitivity and hysteresis in tactile sensors when using soft materials. We discovered that piezoresistive sensors made using an array of three-dimensional (3D) metallic annular cracks on polymeric microstructures possess high sensitivities (> 107Ω ⋅ kPa−1), low hysteresis (2.99 ± 1.37%) over a wide pressure range (0–20 kPa), and fast response (400 Hz). We demonstrate that TRACE sensors can accurately detect and measure the pulse wave velocity (PWV) when skin mounted. Moreover, we show that these tactile sensors when arrayed enabled fast reliable one-touch surface texture classification with neuromorphic encoding and deep learning algorithms.


Author(s):  
M. Boublik ◽  
W. Hellmann ◽  
F. Jenkins

The present knowledge of the three-dimensional structure of ribosomes is far too limited to enable a complete understanding of the various roles which ribosomes play in protein biosynthesis. The spatial arrangement of proteins and ribonuclec acids in ribosomes can be analysed in many ways. Determination of binding sites for individual proteins on ribonuclec acid and locations of the mutual positions of proteins on the ribosome using labeling with fluorescent dyes, cross-linking reagents, neutron-diffraction or antibodies against ribosomal proteins seem to be most successful approaches. Structure and function of ribosomes can be correlated be depleting the complete ribosomes of some proteins to the functionally inactive core and by subsequent partial reconstitution in order to regain active ribosomal particles.


Author(s):  
Robert Glaeser ◽  
Thomas Bauer ◽  
David Grano

In transmission electron microscopy, the 3-dimensional structure of an object is usually obtained in one of two ways. For objects which can be included in one specimen, as for example with elements included in freeze- dried whole mounts and examined with a high voltage microscope, stereo pairs can be obtained which exhibit the 3-D structure of the element. For objects which can not be included in one specimen, the 3-D shape is obtained by reconstruction from serial sections. However, without stereo imagery, only detail which remains constant within the thickness of the section can be used in the reconstruction; consequently, the choice is between a low resolution reconstruction using a few thick sections and a better resolution reconstruction using many thin sections, generally a tedious chore. This paper describes an approach to 3-D reconstruction which uses stereo images of serial thick sections to reconstruct an object including detail which changes within the depth of an individual thick section.


Author(s):  
T.D. Pollard ◽  
P. Maupin

In this paper we review some of the contributions that electron microscopy has made to the analysis of actin and myosin from nonmuscle cells. We place particular emphasis upon the limitations of the ultrastructural techniques used to study these cytoplasmic contractile proteins, because it is not widely recognized how difficult it is to preserve these elements of the cytoplasmic matrix for electron microscopy. The structure of actin filaments is well preserved for electron microscope observation by negative staining with uranyl acetate (Figure 1). In fact, to a resolution of about 3nm the three-dimensional structure of actin filaments determined by computer image processing of electron micrographs of negatively stained specimens (Moore et al., 1970) is indistinguishable from the structure revealed by X-ray diffraction of living muscle.


Author(s):  
J.L. Williams ◽  
K. Heathcote ◽  
E.J. Greer

High Voltage Electron Microscope already offers exciting experimental possibilities to Biologists and Materials Scientists because the increased specimen thickness allows direct observation of three dimensional structure and dynamic experiments on effectively bulk specimens. This microscope is designed to give maximum accessibility and space in the specimen region for the special stages which are required. At the same time it provides an ease of operation similar to a conventional instrument.


Author(s):  
G. E. Tyson ◽  
M. J. Song

Natural populations of the brine shrimp, Artemia, may possess spirochete- infected animals in low numbers. The ultrastructure of Artemia's spirochete has been described by conventional transmission electron microscopy. In infected shrimp, spirochetal cells were abundant in the blood and also occurred intra- and extracellularly in the three organs examined, i.e. the maxillary gland (segmental excretory organ), the integument, and certain muscles The efferent-tubule region of the maxillary gland possessed a distinctive lesion comprised of a group of spirochetes, together with numerous small vesicles, situated in a cave-like indentation of the base of the tubule epithelium. in some instances the basal lamina at a lesion site was clearly discontinuous. High-voltage electron microscopy has now been used to study lesions of the efferent tubule, with the aim of understanding better their three-dimensional structure.Tissue from one maxillary gland of an infected, adult, female brine shrimp was used for HVEM study.


Author(s):  
Jerome J. Paulin

Within the past decade it has become apparent that HVEM offers the biologist a means to explore the three-dimensional structure of cells and/or organelles. Stereo-imaging of thick sections (e.g. 0.25-10 μm) not only reveals anatomical features of cellular components, but also reduces errors of interpretation associated with overlap of structures seen in thick sections. Concomitant with stereo-imaging techniques conventional serial Sectioning methods developed with thin sections have been adopted to serial thick sections (≥ 0.25 μm). Three-dimensional reconstructions of the chondriome of several species of trypanosomatid flagellates have been made from tracings of mitochondrial profiles on cellulose acetate sheets. The sheets are flooded with acetone, gluing them together, and the model sawed from the composite and redrawn.The extensive mitochondrial reticulum can be seen in consecutive thick sections of (0.25 μm thick) Crithidia fasciculata (Figs. 1-2). Profiles of the mitochondrion are distinguishable from the anterior apex of the cell (small arrow, Fig. 1) to the posterior pole (small arrow, Fig. 2).


Author(s):  
Kenneth H. Downing ◽  
Hu Meisheng ◽  
Hans-Rudolf Went ◽  
Michael A. O'Keefe

With current advances in electron microscope design, high resolution electron microscopy has become routine, and point resolutions of better than 2Å have been obtained in images of many inorganic crystals. Although this resolution is sufficient to resolve interatomic spacings, interpretation generally requires comparison of experimental images with calculations. Since the images are two-dimensional representations of projections of the full three-dimensional structure, information is invariably lost in the overlapping images of atoms at various heights. The technique of electron crystallography, in which information from several views of a crystal is combined, has been developed to obtain three-dimensional information on proteins. The resolution in images of proteins is severely limited by effects of radiation damage. In principle, atomic-resolution, 3D reconstructions should be obtainable from specimens that are resistant to damage. The most serious problem would appear to be in obtaining high-resolution images from areas that are thin enough that dynamical scattering effects can be ignored.


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