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Biomems
Published in Simona Badilescu, Muthukumaran Packirisamy, BioMEMS, 2016
Simona Badilescu, Muthukumaran Packirisamy
Troponin C is considered the primary biomarker for myocardial injury, and the study of its interaction with membrane proteins is of considerable importance. In the present work, an optical lever method is employed to study the interaction of rabbit skeletal muscle troponin C (TnC) with a twenty-six-residue membrane protein (ME). The cantilever deflection is measured for different concentrations, as shown in Figures 9.88 and 9.89. These figures present the tip deflection of the cantilever as the interaction progresses, after TnC-ME is allowed to interact on the microcantilever. It is interesting to notice the change in direction for the deflection. The results show the unique pattern of deflection that characterizes the TnC-ME biomechanical interaction. The reversal of deflection also indicates the reversal of stresses produced during biomechanical interactions. One could identify the variation from compressive stress to tensile surface stress during the biointeractions. In addition, the peak deflection could also be used to measure the concentration, as the amplitude of deflection was found to be proportional to the concentration, as shown in Figure 9.90. This deflection pattern becomes the unique signature that is specific for the TnC-ME interaction.
Nanopharmaceuticals in Cardiovascular Medicine
Published in Harishkumar Madhyastha, Durgesh Nandini Chauhan, Nanopharmaceuticals in Regenerative Medicine, 2022
Ramandeep Singh, Anupam Mittal, Maryada Sharma, Ajay Bahl, Madhu Khullar
Troponins are a group of proteins found in the cardiac muscles and skeletal muscles that help to control and regulate the contraction of the muscles. There are three variants of the protein troponin, i.e., troponin I, troponin C, and troponin T. In case of cardiovascular diseases where cardiomyocytes are damaged, troponin C and troponin I are expressed in higher quantities in blood. The levels of both troponin C and troponin I are undetectable in normal conditions; therefore, they serve as potential biomarkers for cardiovascular diseases. Efforts are being made into developing these two biomolecules into biomarkers (Park et al., 2020).
Agrochemical-mediated cardiotoxicity in zebrafish embryos/larvae: What we do and where we go
Published in Critical Reviews in Environmental Science and Technology, 2023
Yang Yang, Yue Tao, Zixu Li, Yunhe Cui, Jinzhu Zhang, Ying Zhang
Ca2+ is essential for cardiac contraction and diastole, and imbalances in Ca2+ homeostasis in cardiomyocytes are often an important trigger of cardiac failure (Li & Hwang, 2015). Briefly, activation of voltage-dependent L-type Ca channels (DHP receptors) upon membrane depolarization causes Ca2+ enter into the cytoplasmic matrix and activate RYR2 via a Ca2+-induced Ca release mechanism, causing the release of Ca2+ from the sarcoplasmic reticulum (SR) and binding of Ca2+ to troponin C and ultimately myocardial contraction (Eisner et al., 2017). Continuous contraction of the myocardium cannot cause periodic beating of cardiac cells, and myocardial diastole occurs when the Ca2+ bound to troponin C is pumped out of the cell by the Na+/Ca2+ exchanger or pumped back into the SR by the sarco(endo)plasmic Ca2+-ATPase in the nonfunctional region of the SR (Bovo et al., 2013) (Figure 5).
A novel colorimetric assay for calcium ion and calmodulin detection based on gold nanoparticles
Published in Inorganic and Nano-Metal Chemistry, 2020
Until now, the most of the reported approaches for Ca2+ or calmodulin detection are mostly introducing some optical sensitive Ca2+ probe to monitor the fluorescent changes of probe.[10–15] Generally, these fluorescent probes are some special fluorogen with Ca2+ ion recognition, and show some fluorescent changes response to Ca2+. For instance, Yuan et al. demonstrated a graphene oxide-cationic conjugated polymer hybrid probe for calmodulin sensing.[10] Nagai et al. designed a spectral palette of fluorescent protein as Ca2+ indicators that could recognized Ca2+ with up to three distinct colors.[11] Barykina et al. proposed a two-fluorophore-based sensor, carrying opsanus troponin C as the Ca2+-binding moiety, and provided a linear response to Ca2+ ions.[14] However, these reported probes are faced with the complex synthetic process and expensive cost, which hampered their large-scale application. Therefore, it is still a challenge to develop a simple, easy-to-operate, inexpensive, and high-throughput assay for Ca2+ and calmodulin detection. Visual assay is an idea analysis technology that can translate the recognition event into a visual color change.