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Raman Spectroscopic Imaging Analysis of Signaling Proteins and Protein Cofactors in Living Cells

Silwal, Achut Prasad, -
http://orcid.org/0000-0003-0271-5723
http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1528721394633565

Abstract Details

2018, Doctor of Philosophy (Ph.D.), Bowling Green State University, Photochemical Sciences.
Proteins play a central role in biological processes. Broad classes of protein types are involved in the innumerable functions of living systems, such as catalysis of the biochemical reactions, transportation of the essential molecules, defense of the immune system, and the transmission of messages from cells to cells. In our projects, we have combined the analytical approaches including surface-enhanced Raman scattering (SERS), fluorescence microscopy, electrochemistry, and computational methods to investigate the structures and functions of the proteins and signaling molecules in the living cells. In our research, we have studied the interactions and functions of dopamine transporters (DAT), dopamine receptors (DARs), and several signaling molecules such as dopamine (DA), amphetamine (AMP), methamphetamine (MAMP), and methylenedioxypyrovalerone (MDPV) in living cells. The interactions between signaling molecules and DAT or DARs are crucial for the functioning of dopaminergic pathways. In our project, we have probed interactions of signaling proteins including DAT and DARs and investigated the changes that happen in signaling proteins, other interacting compounds or intracellular contents of the second messenger such as cyclic adenosine monophosphate (cAMP). The second messenger like cAMP is important in many biological processes which are produced due to interactions of the signaling protein in living cells. Our studies on DA-DAT or DA-DARs interactions mainly utilize the Raman spectroscopy to characterize the selectivity and efficacy of psychopharmaceutic drugs. In addition, we have also studied the redox states and mechanism of protein cofactors in different experimental conditions. We have probed and characterized the redox states and mechanisms of FMN cofactors in biological and non-biological environments using electrochemistry, SERS measurements, and computational measurements. The results obtained from our research could be useful in the diagnosis of abnormalities or diseases originated from malfunctioning of proteins or protein-ligand interactions.
H Peter Lu, PhD (Advisor)
John R Cable, PhD (Committee Member)
Alexey T Zayak, PhD (Committee Member)
Anita Simic, PhD (Other)
236 p.
Chemistry
Dopamine; Mode-selective Raman imaging; Human dopamine transporter; HEK293 cell; DA-hDAT interaction; FMN redox states; flavin coenzyme; electrochemical redox mechanism; SERS spectroscopy

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Citations

  • Silwal, -, A. P. (2018). Raman Spectroscopic Imaging Analysis of Signaling Proteins and Protein Cofactors in Living Cells [Doctoral dissertation, Bowling Green State University]. OhioLINK Electronic Theses and Dissertations Center. http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1528721394633565

    APA Style (7th edition)

  • Silwal, -, Achut. Raman Spectroscopic Imaging Analysis of Signaling Proteins and Protein Cofactors in Living Cells . 2018. Bowling Green State University, Doctoral dissertation. OhioLINK Electronic Theses and Dissertations Center, http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1528721394633565.

    MLA Style (8th edition)

  • Silwal, -, Achut. "Raman Spectroscopic Imaging Analysis of Signaling Proteins and Protein Cofactors in Living Cells ." Doctoral dissertation, Bowling Green State University, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1528721394633565

    Chicago Manual of Style (17th edition)

bgsu1528721394633565
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© 2018, some rights reserved.Creative Commons License Raman Spectroscopic Imaging Analysis of Signaling Proteins and Protein Cofactors in Living Cells by Achut Prasad Silwal - is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 3.0 Unported License. Based on a work at etd.ohiolink.edu.
This open access ETD is published by Bowling Green State University and OhioLINK.