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Development of High Throughput Metho...

University of California, Riverside., Chemistry.

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Development of High Throughput Methods for Probing Biomacromolecular Interactions.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Development of High Throughput Methods for Probing Biomacromolecular Interactions./
Author:	Ashby, Jonathan Tyrone.
Description:	211 p.
Notes:	Source: Dissertation Abstracts International, Volume: 75-11(E), Section: B.
Contained By:	Dissertation Abstracts International75-11B(E).
Subject:	Analytical chemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3630644
ISBN:	9781321086836

Development of High Throughput Methods for Probing Biomacromolecular Interactions.
Ashby, Jonathan Tyrone.

Development of High Throughput Methods for Probing Biomacromolecular Interactions. - 211 p.

Source: Dissertation Abstracts International, Volume: 75-11(E), Section: B.

Thesis (Ph.D.)--University of California, Riverside, 2014.

This item is not available from ProQuest Dissertations & Theses.

Within living organisms, there exists a large variety of macromolecular interactions, such as protein-protein, nucleic acid-protein, or lipid-protein. Also known as the interactome, these interactions are essential to a variety of functions, such as gene regulation and internal/external cell signaling. Engineered nanomaterials (ENMs) have gained increased popularity in recent years as a tool for biosensing and bioanalysis. However, little is known about how these ENMs could adversely affect the interactome, either through intentional or accidental exposure to ENMs.

ISBN: 9781321086836Subjects--Topical Terms:

3168300
Analytical chemistry.

Development of High Throughput Methods for Probing Biomacromolecular Interactions.
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020 $a 9781321086836
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100 1 $a Ashby, Jonathan Tyrone. $3 3174091
245 1 0 $a Development of High Throughput Methods for Probing Biomacromolecular Interactions.
300 $a 211 p.
500 $a Source: Dissertation Abstracts International, Volume: 75-11(E), Section: B.
500 $a Adviser: Wenwan Zhong.
502 $a Thesis (Ph.D.)--University of California, Riverside, 2014.
506 $a This item is not available from ProQuest Dissertations & Theses.
506 $a This item must not be sold to any third party vendors.
520 $a Within living organisms, there exists a large variety of macromolecular interactions, such as protein-protein, nucleic acid-protein, or lipid-protein. Also known as the interactome, these interactions are essential to a variety of functions, such as gene regulation and internal/external cell signaling. Engineered nanomaterials (ENMs) have gained increased popularity in recent years as a tool for biosensing and bioanalysis. However, little is known about how these ENMs could adversely affect the interactome, either through intentional or accidental exposure to ENMs.
520 $a A powerful tool for probing macromolecular interactions is flow field-flow fractionation (F4), and its successor, asymmetrical F4 (AF4). (A)F4 is an open channel separation technique that fractionates analytes based purely on their size. Similarly to other open channel techniques like size exclusion chromatography and capillary electrophoresis, (A)F4 is well suited to preserving the native structure of the macromolecular complex. F4 was used to differentiate between the stable and transient protein coronas surrounding ENMs as they enter a biological matrix. Analysis of the isolated ENM-protein coronas has revealed correlations between the nature of the surface coating (hydropathy, charge density) and the composition of the stable and transient corona.
520 $a Due to the batch-to-batch variability of ENM synthesis, tools are also needed to rapidly assess how changes in the size, shape or surface coating may adversely affect the behavior of ENMs within the body. A fluorescence assay was designed to take advantage of changes in a protein's tertiary structure upon interaction with a nanoparticle to determine the effects of changes in an ENM's physiochemical parameters.
520 $a Finally, an AF4 method was designed for the fractionation of micro RNA (miRNA) into fractions such as small protein-bound, lipoprotein complex-bound, and exosomal. Changes in miRNA levels within the body can be used for early disease detection. By correlating up and down-regulation of miRNA with increased/decreased concentrations of particular proteins, identification of associated protein biomarkers can be done. If these protein markers exist in higher concentrations within the body, changes in this protein level could be used as a guide to direct additional testing for specific miRNA biomarkers.
590 $a School code: 0032.
650 4 $a Analytical chemistry. $3 3168300
650 4 $a Nanotechnology. $3 526235
690 $a 0486
690 $a 0652
710 2 $a University of California, Riverside. $b Chemistry. $3 1682435
773 0 $t Dissertation Abstracts International $g 75-11B(E).
790 $a 0032
791 $a Ph.D.
792 $a 2014
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3630644