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MOF-based Electrochemical Sensors for Protein Detection
Published in Ram K. Gupta, Tahir Rasheed, Tuan Anh Nguyen, Muhammad Bilal, Metal-Organic Frameworks-Based Hybrid Materials for Environmental Sensing and Monitoring, 2022
Yang Liu, Juanhua Zhou, Shiyu Zhang, Hongye Wang
Protein kinase is a kind of enzyme that catalyzes the process of protein phosphorylation. Its activity is closely related to various diseases. Therefore, the detection of protein kinase activity in clinical diagnosis can help diagnosis. Song et al. proposed a low fouling and highly sensitive electrochemical sensor for T4 polynucleotide kinase (PNK) detection based on zwitterionic peptide and self-sacrificial Fe-MOF [67]. The zwitterionic peptide could be assembled into antifouling layers and the Fe-MOF formed Prussian blue (PB) after reacting with K4Fe(CN)6. Thus, the biosensor prevented the adsorption of nonspecific proteins and had a high sensitivity. Another kinase, protein tyrosine kinase-7 (PTK7) could also be detected by an electrochemical biosensor based on Zn-MOF-on-Zr-MOF architecture [33]. In addition to electrochemical biosensors, photoelectrochemical biosensors attracted lots of interest as well. Our team developed a highly sensitive photoelectrochemical biosensor for the detection of protein kinase A (PKA) by Ru(bpy)32+ loaded UiO-66 (Ru(bpy)32+@UiO-66) [44]. UiO-66 not only increased the load of Ru(bpy)32+ but also provided a large number of phosphorylated kemptide binding sites. Therefore, the biosensor achieved high sensitivity and fast response.
Synapses
Published in Nassir H. Sabah, Neuromuscular Fundamentals, 2020
The phosphate group is hydrolyzed back to an OH– group by enzymes referred to as phosphatases, and the process is known as dephosphorylation. Protein phosphatase 1 (PP1) dephosphorylates a variety of proteins as well as K+ and Ca2+ channels, NMDA, and AMPA glutamate receptors. Protein phosphatase 2A (PP2A) also dephosphorylates a range of proteins that overlap with those of PP1, in addition to tau protein that stabilizes microtubules of the cytoskeleton. Excessive phosphorylation of tau protein is associated with Alzheimer’s disease. Protein phosphatase 2B (PP2B), also known as calcineurin, is abundant in neurons and is activated by Ca2+. It activates T cells of the immune system and dephosphorylates AMPA receptors. Protein phosphorylation and dephosphorylation are of fundamental importance in cell functioning as it is the major molecular mechanism through which protein activity in a cell is regulated both in and outside the nervous system.
Proteins and Proteomics
Published in Firdos Alam Khan, Biotechnology Fundamentals, 2020
During cell signaling, many enzymes and structural proteins undergo phosphorylation. The addition of a phosphate to amino acids, most commonly serine and threonine mediated by serine or threonine kinases, or more rarely tyrosine mediated by tyrosine kinases, causes a protein to become a target for binding or interacting with a distinct set of other proteins that recognize the phosphorylated domain. Because protein phosphorylation is one of the most-studied protein modifications, many “proteomics” efforts are geared to determining the set of phosphorylated proteins in a specific cell or tissue-type under specific circumstances.
Smart polymers driven by multiple and tunable hydrogen bonds for intact phosphoprotein enrichment
Published in Science and Technology of Advanced Materials, 2019
Xiaofei Zhang, Qi Lu, Cheng Chen, Xiuling Li, Guangyan Qing, Taolei Sun, Xinmiao Liang
Protein phosphorylation is a specific and reversible post-translational modification, which regulates numerous biological events, such as signal transduction, gene expression, and the cell cycle [1,2]. Substantial studies have revealed the close relationships between abnormal protein phosphorylation and aberrant protein functions, which subsequently lead to many critical diseases (i.e. cancers [3,4] and neurodegenerative diseases [5]). Thus, phosphorylated proteins have attracted increasing interest of scientists working in biology, pathology and therapeutics.