Study of Passive and Active Magnetic Levitation Bearings for Implementation in Pediatric Left Ventricle Assistant Device



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Kinase Probes (KP) are molecules that can modify the activities of proteins selectively. The use of a KP is significant because it allows researchers to see how the KP interacts with the target protein mechanistically in vitro or in vivo. The electrophile is a valuable component of a KP. The electrophile must be capable of forming a covalent bond with the catalytic lysine of a PK. When the catalytic lysine is targeted and the kinase site is activated, the PK's stabilization becomes dependent on it. The electrophile must be chosen carefully when targeting the catalytic lysine. A component of KP, a compound we are developing, binds to numerous kinases. However, known electrophiles, such as sulfonyl fluorides probes, are thought to be overly reactive. We don't want to have a KP that only reacts with tyrosine-protein kinase. The question of whether the electrophile only covalently binds to the lysine on Cyclin-dependent kinase 5 (CDK5) or whether the electrophile can also form a bond with other kinases arises during the development of this electrophile that is expected to target the catalytic lysine. In addition to this, fluorine screening concerning different mono-, di-, and tri-fluorine substitution reactions are what we are performing as well. Because of the high sensitivity of the 19F nuclei found in nuclear magnetic resonance (NMR) measurements, many fluorinated molecules are used in pharmaceuticals. According to many studies, about a third of new approved drugs contain fluorine atoms or fluoroalkyl groups. Additionally, fluorine substitution reactions affect kinetic activity. This project was completed with contributions from Victor Tesesco and Yaxin Wang from the Texas Heart Institute.



Mechanical Engineering