Fluoro-Silane as a Functional Monomer for Protein Conformational Imprinting

By using the technology of molecularly imprinted polymer (MIP), we propose to synthesize a protein conformational imprint that also acts as a plastic enzyme, inducing protein structural transitions. The imprint aims at MIP-induced stabilization and / or formation of bound protein secondary structure...

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Main Author: Peng, Yun
Format: Others
Published: DigitalCommons@USU 2011
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Online Access:https://digitalcommons.usu.edu/etd/906
https://digitalcommons.usu.edu/cgi/viewcontent.cgi?article=1902&context=etd
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spelling ndltd-UTAHS-oai-digitalcommons.usu.edu-etd-19022019-10-13T05:37:58Z Fluoro-Silane as a Functional Monomer for Protein Conformational Imprinting Peng, Yun By using the technology of molecularly imprinted polymer (MIP), we propose to synthesize a protein conformational imprint that also acts as a plastic enzyme, inducing protein structural transitions. The imprint aims at MIP-induced stabilization and / or formation of bound protein secondary structure and the applications associated with analysis and correction of misfolded proteins. The screening of polymeric functional monomers being able to induce the conformational transitions in proteins is investigated in this report. The fluoro-silanes (3-heptafluoroisopropoxy)propalethoxysilane (7F) and 3,3,3-trifluoropropylmethoxysilane (3F) were employed as functional monomers for synthesis of this catalytic protein conformational imprint via sol-gel reactions. 3F was demonstrated superior to 7F for fluoro-modification of tetraethylorthosilicate (TEOS) gel in terms of retaining gel transparency and increasing hydrophobicity while maintaining a uniform distribution of encapsulated protein. Both hydrolyzed 3F and polymerized 3F exhibited strong influences on structure transitions of three template proteins: bovine serum albumin (BSA), beta-lactoglobulin (BLG), and bovine carbonic anhydrase (BCA). The formation of molten globule intermediates that stabilized by increased alpha-helices was induced by the trifluoro-silane in BLG and BCA. Additionally, 3F was effective at a lower concentration than the benchmark fluoro-alcohol 1,1,1,3,3,3-hexafluoro-2-propanol (HFIP), validating the application of 3F as a functional monomer for protein conformational imprinting. 2011-05-01T07:00:00Z text application/pdf https://digitalcommons.usu.edu/etd/906 https://digitalcommons.usu.edu/cgi/viewcontent.cgi?article=1902&context=etd Copyright for this work is held by the author. Transmission or reproduction of materials protected by copyright beyond that allowed by fair use requires the written permission of the copyright owners. Works not in the public domain cannot be commercially exploited without permission of the copyright owner. Responsibility for any use rests exclusively with the user. For more information contact Andrew Wesolek (andrew.wesolek@usu.edu). All Graduate Theses and Dissertations DigitalCommons@USU functional monomer molecularly imprinted polymer protein conformational imprinting Biomedical Engineering and Bioengineering
collection NDLTD
format Others
sources NDLTD
topic functional monomer
molecularly imprinted polymer
protein conformational imprinting
Biomedical Engineering and Bioengineering
spellingShingle functional monomer
molecularly imprinted polymer
protein conformational imprinting
Biomedical Engineering and Bioengineering
Peng, Yun
Fluoro-Silane as a Functional Monomer for Protein Conformational Imprinting
description By using the technology of molecularly imprinted polymer (MIP), we propose to synthesize a protein conformational imprint that also acts as a plastic enzyme, inducing protein structural transitions. The imprint aims at MIP-induced stabilization and / or formation of bound protein secondary structure and the applications associated with analysis and correction of misfolded proteins. The screening of polymeric functional monomers being able to induce the conformational transitions in proteins is investigated in this report. The fluoro-silanes (3-heptafluoroisopropoxy)propalethoxysilane (7F) and 3,3,3-trifluoropropylmethoxysilane (3F) were employed as functional monomers for synthesis of this catalytic protein conformational imprint via sol-gel reactions. 3F was demonstrated superior to 7F for fluoro-modification of tetraethylorthosilicate (TEOS) gel in terms of retaining gel transparency and increasing hydrophobicity while maintaining a uniform distribution of encapsulated protein. Both hydrolyzed 3F and polymerized 3F exhibited strong influences on structure transitions of three template proteins: bovine serum albumin (BSA), beta-lactoglobulin (BLG), and bovine carbonic anhydrase (BCA). The formation of molten globule intermediates that stabilized by increased alpha-helices was induced by the trifluoro-silane in BLG and BCA. Additionally, 3F was effective at a lower concentration than the benchmark fluoro-alcohol 1,1,1,3,3,3-hexafluoro-2-propanol (HFIP), validating the application of 3F as a functional monomer for protein conformational imprinting.
author Peng, Yun
author_facet Peng, Yun
author_sort Peng, Yun
title Fluoro-Silane as a Functional Monomer for Protein Conformational Imprinting
title_short Fluoro-Silane as a Functional Monomer for Protein Conformational Imprinting
title_full Fluoro-Silane as a Functional Monomer for Protein Conformational Imprinting
title_fullStr Fluoro-Silane as a Functional Monomer for Protein Conformational Imprinting
title_full_unstemmed Fluoro-Silane as a Functional Monomer for Protein Conformational Imprinting
title_sort fluoro-silane as a functional monomer for protein conformational imprinting
publisher DigitalCommons@USU
publishDate 2011
url https://digitalcommons.usu.edu/etd/906
https://digitalcommons.usu.edu/cgi/viewcontent.cgi?article=1902&context=etd
work_keys_str_mv AT pengyun fluorosilaneasafunctionalmonomerforproteinconformationalimprinting
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