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Targeting RNA with small molecules.

Schirle, Nicole Therese.

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Targeting RNA with small molecules.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Targeting RNA with small molecules./
作者:	Schirle, Nicole Therese.
面頁冊數:	149 p.
附註:	Source: Masters Abstracts International, Volume: 49-02, page: 1190.
Contained By:	Masters Abstracts International49-02.
標題:	Chemistry, Biochemistry. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=1482854
ISBN:	9781124318868

Targeting RNA with small molecules.
Schirle, Nicole Therese.

Targeting RNA with small molecules. - 149 p.

Source: Masters Abstracts International, Volume: 49-02, page: 1190.

Thesis (M.S.)--University of California, Davis, 2010.

RNA serves many vital functions in biology. Therefore, the design of RNA-binding small molecules would serve as important tools for the study of gene expression and RNA interference. A major aim of this thesis work is the design of quinoline-based helix-threading peptides (HTPs) that can bind double-stranded RNA via threading intercalation. Ring closing metathesis was used to generate a small library of cyclic HTPs, which vary in peptide sequence and stereochemistry of the alpha-carbon of amino acid residues. A thiazole orange displacement assay was developed for screening HTP binding to an in vitro selected RNA aptamer binding site. Results showed that binding affinity is dependent on peptide sequence and amino acid stereochemistry.

ISBN: 9781124318868Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

Targeting RNA with small molecules.
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500 $a Adviser: Peter A. Beal.
502 $a Thesis (M.S.)--University of California, Davis, 2010.
520 $a RNA serves many vital functions in biology. Therefore, the design of RNA-binding small molecules would serve as important tools for the study of gene expression and RNA interference. A major aim of this thesis work is the design of quinoline-based helix-threading peptides (HTPs) that can bind double-stranded RNA via threading intercalation. Ring closing metathesis was used to generate a small library of cyclic HTPs, which vary in peptide sequence and stereochemistry of the alpha-carbon of amino acid residues. A thiazole orange displacement assay was developed for screening HTP binding to an in vitro selected RNA aptamer binding site. Results showed that binding affinity is dependent on peptide sequence and amino acid stereochemistry.
520 $a Despite RNA mapping with EDTA-Fe modified HTPs, little is known about the contacts HTPs make with their RNA targets. A self-complementary single strand of RNA was designed to anneal with itself forming two HTP binding sites. In collaboration with Professor Andrew Fisher, crystals of an HTP/RNA complex diffracted to 2.95 A at Stanford Synchrotron Radiation Lightsource (SSRL). Furthermore, the RNA-binding domain of the U1A spliceosomal protein was expressed and purified for use in aptamer crystallization.
520 $a Moreover, we have moved away from in vitro selected aptamers to focus on an mRNA coding for the serotonin 5HT2C receptor protein. This RNA made an interesting HTP target for two reasons: (1) it is an adenosine-to-inosine RNA editing substrate, and (2) it should have a binding site for HTPs. A short duplex RNA containing several editing sites and loop region likely to be a target for HTPs was designed for quantitative S1 footprinting. We utilized hydroxyl radical affinity cleavage to characterize binding specificity of cyclic HTPs for this RNA target and found that cyclic HTPs selectively target the serotonin RNA. Furthermore, cyclic HTPs were shown to bind the serotonin RNA and were capable of substrate-selective inhibition of RNA editing.
520 $a Finally, the pre-mRNA coding for the DNA repair enzyme Neil1 was shown to be a substrate the adenosine deaminase that acts on RNA 1 (ADAR1). Editing of this novel substrate was characterized and treatment of glioma cells with interferon resulted in increased editing of Neil1 pre-mRNA in vivo .
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