scholarly journals Validation of Fabric-Based Thigh-Wearable EMG Sensors and Oximetry for Monitoring Quadriceps Activity during Strength and Endurance Exercises

Sensors ◽  
2020 ◽  
Vol 20 (17) ◽  
pp. 4664
Author(s):  
Riccardo Di Giminiani ◽  
Marco Cardinale ◽  
Marco Ferrari ◽  
Valentina Quaresima
Keyword(s):  
Gold Standard ◽  
Near Infrared ◽  
Objective Assessment ◽  
Muscular Activity ◽  
Quadriceps Muscle ◽  
Surface Emg ◽  
Oxyhemoglobin Saturation ◽  
Muscle Groups ◽  
Regional Muscle

Muscle oximetry based on near-infrared spectroscopy (NIRS) and electromyography (EMG) techniques in adherent clothing might be used to monitor the muscular activity of selected muscle groups while exercising. The fusion of these wearable technologies in sporting garments can allow the objective assessment of the quality and the quantity of the muscle activity as well as the continuous monitoring of exercise programs. Several prototypes integrating EMG and NIRS have been developed previously; however, most devices presented the limitations of not measuring regional muscle oxyhemoglobin saturation and did not embed textile sensors for EMG. The purpose of this study was to compare regional muscle oxyhemoglobin saturation and surface EMG data, measured under resting and dynamic conditions (treadmill run and strength exercises) by a recently developed wearable integrated quadriceps muscle oximetry/EMG system adopting smart textiles for EMG, with those obtained by using two “gold standard” commercial instrumentations for EMG and muscle oximetry. The validity and agreement between the wearable integrated muscle oximetry/EMG system and the “gold standard” instrumentations were assessed by using the Bland-Altman agreement plots to determine the bias. The results support the validity of the data provided by the wearable electronic garment developed purposely for the quadriceps muscle group and suggest the potential of using such device to measure strength and endurance exercises in vivo in various populations.

Fluorescent proteins for in vivo imaging, where's the biliverdin?

2020 ◽  
Vol 48 (6) ◽  
pp. 2657-2667
Author(s):  
Felipe Montecinos-Franjola ◽  
John Y. Lin ◽  
Erik A. Rodriguez
Keyword(s):  
Hydrogen Peroxide ◽  
In Vivo Imaging ◽  
Near Infrared ◽  
Fluorescent Protein ◽  
Fluorescent Proteins ◽  
Fluorescent Imaging ◽  
Infrared Light ◽  
Red Fluorescent Protein ◽  
Color Palette

Noninvasive fluorescent imaging requires far-red and near-infrared fluorescent proteins for deeper imaging. Near-infrared light penetrates biological tissue with blood vessels due to low absorbance, scattering, and reflection of light and has a greater signal-to-noise due to less autofluorescence. Far-red and near-infrared fluorescent proteins absorb light >600 nm to expand the color palette for imaging multiple biosensors and noninvasive in vivo imaging. The ideal fluorescent proteins are bright, photobleach minimally, express well in the desired cells, do not oligomerize, and generate or incorporate exogenous fluorophores efficiently. Coral-derived red fluorescent proteins require oxygen for fluorophore formation and release two hydrogen peroxide molecules. New fluorescent proteins based on phytochrome and phycobiliproteins use biliverdin IXα as fluorophores, do not require oxygen for maturation to image anaerobic organisms and tumor core, and do not generate hydrogen peroxide. The small Ultra-Red Fluorescent Protein (smURFP) was evolved from a cyanobacterial phycobiliprotein to covalently attach biliverdin as an exogenous fluorophore. The small Ultra-Red Fluorescent Protein is biophysically as bright as the enhanced green fluorescent protein, is exceptionally photostable, used for biosensor development, and visible in living mice. Novel applications of smURFP include in vitro protein diagnostics with attomolar (10−18 M) sensitivity, encapsulation in viral particles, and fluorescent protein nanoparticles. However, the availability of biliverdin limits the fluorescence of biliverdin-attaching fluorescent proteins; hence, extra biliverdin is needed to enhance brightness. New methods for improved biliverdin bioavailability are necessary to develop improved bright far-red and near-infrared fluorescent proteins for noninvasive imaging in vivo.

scholarly journals Real-time observation of tetrapyrrole binding to an engineered bacterial phytochrome

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Yusaku Hontani ◽  
Mikhail Baloban ◽  
Francisco Velazquez Escobar ◽  
Swetta A. Jansen ◽  
Daria M. Shcherbakova ◽  
...  
Keyword(s):  
Real Time ◽  
Rational Design ◽  
Near Infrared ◽  
Fluorescent Proteins ◽  
Covalent Bond ◽  
Binding Pocket ◽  
Tissue Imaging ◽  
Covalent Attachment ◽  
Time Resolved

AbstractNear-infrared fluorescent proteins (NIR FPs) engineered from bacterial phytochromes are widely used for structural and functional deep-tissue imaging in vivo. To fluoresce, NIR FPs covalently bind a chromophore, such as biliverdin IXa tetrapyrrole. The efficiency of biliverdin binding directly affects the fluorescence properties, rendering understanding of its molecular mechanism of major importance. miRFP proteins constitute a family of bright monomeric NIR FPs that comprise a Per-ARNT-Sim (PAS) and cGMP-specific phosphodiesterases - Adenylyl cyclases - FhlA (GAF) domain. Here, we structurally analyze biliverdin binding to miRFPs in real time using time-resolved stimulated Raman spectroscopy and quantum mechanics/molecular mechanics (QM/MM) calculations. Biliverdin undergoes isomerization, localization to its binding pocket, and pyrrolenine nitrogen protonation in <1 min, followed by hydrogen bond rearrangement in ~2 min. The covalent attachment to a cysteine in the GAF domain was detected in 4.3 min and 19 min in miRFP670 and its C20A mutant, respectively. In miRFP670, a second C–S covalent bond formation to a cysteine in the PAS domain occurred in 14 min, providing a rigid tetrapyrrole structure with high brightness. Our findings provide insights for the rational design of NIR FPs and a novel method to assess cofactor binding to light-sensitive proteins.

Gram-scale synthesis of a neodymium chelate as a spectral CT and second near-infrared window imaging agent for visualizing the gastrointestinal tract in vivo

2021 ◽  
Author(s):  
Pengrui Zhuang ◽  
Ke Xiang ◽  
Xiangxi Meng ◽  
Guohe Wang ◽  
Ziyuan Li ◽  
...  
Keyword(s):  
Gastrointestinal Tract ◽  
Fluorescence Imaging ◽  
Large Scale ◽  
Near Infrared ◽  
Imaging Agent ◽  
Spectral Ct ◽  
Green Method ◽  
Infrared Window

A facile and green method was developed to fabricate Nd-DTPA on a large scale without byproducts for CT/spectral CT and NIR II fluorescence imaging of the gastrointestinal tract in vivo.

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