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Engineering protein-based biomateria...

Williams, Danielle Marie.

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Engineering protein-based biomaterials using SpyTag/SpyCatcher technology.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Engineering protein-based biomaterials using SpyTag/SpyCatcher technology./
作者:	Williams, Danielle Marie.
出版者:	Ann Arbor : ProQuest Dissertations & Theses, : 2018,
面頁冊數:	125 p.
附註:	Source: Dissertations Abstracts International, Volume: 80-02, Section: B.
Contained By:	Dissertations Abstracts International80-02B.
標題:	Biochemistry. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10957209
ISBN:	9780438269507

Engineering protein-based biomaterials using SpyTag/SpyCatcher technology.
Williams, Danielle Marie.

Engineering protein-based biomaterials using SpyTag/SpyCatcher technology. - Ann Arbor : ProQuest Dissertations & Theses, 2018 - 125 p.

Source: Dissertations Abstracts International, Volume: 80-02, Section: B.

Thesis (Ph.D.)--Yale University, 2018.

This item must not be added to any third party search indexes.

The ability to create linkages using SpyTag/SpyCatcher technology is a powerful tool for protein design and engineering. SpyTag, a 13-residue peptide, and SpyCatcher, a small protein, interact spontaneously to form a covalent isopeptide bond, which has great potential for use in the design of self-assembling materials. Here we exploit the desirable properties of SpyTag/SpyCatcher in addition to other protein building blocks to develop new protein-based materials with biomedical applications. One such project involves the design of stimulus-responsive hydrogels made entirely of protein components. We took advantage of the modular nature of TPR domains, which bind C-terminal peptides, to interact with cognate peptide cross-linkers to form an ionic hydrogel network. Through the adaptation of SpyTag/SpyCatcher technology, we have developed a concatenation scheme that allows us to create branched protein topologies with multivalent peptides that correspond to TPR domains. By mixing telechelic peptide cross-linkers with their corresponding TPR arrays, we demonstrate the formation of hydrogels that can respond to a physiological stimulus. Other projects described in this text involve the development of geometric protein arrays. Such arrays have implications in signal amplification, biosensing, and enzyme scaffolding array. Using the modular, rod-like protein SasG and SpyTag/SpyCatcher technology, we were able to create discrete rectangular protein arrays with tunable dimensions. In a different project, SpyCatcher arrays were used to create complexes that can display various numbers of recognition elements on the same construct. As a proof of principle, we designed complexes that can bind to HER2, a relevant breast cancer biomarker. Finally, we were able to functionalize 2D surfaces and microcapsules using SpyTag/SpyCatcher technology and a unique, amphiphilic bacterial hydrophobin, Bs1A. Bs1A self-assembles into a stable monolayer at both air-water and water-oil interfaces. We have functionalized these proteins with SpyTag and SnoopTag for use in decorating surfaces and microcapsules with proteins of interest attached to SpyCatcher.

ISBN: 9780438269507Subjects--Topical Terms:

518028
Biochemistry.
Subjects--Index Terms:

Biomaterials

Engineering protein-based biomaterials using SpyTag/SpyCatcher technology.
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520 $a The ability to create linkages using SpyTag/SpyCatcher technology is a powerful tool for protein design and engineering. SpyTag, a 13-residue peptide, and SpyCatcher, a small protein, interact spontaneously to form a covalent isopeptide bond, which has great potential for use in the design of self-assembling materials. Here we exploit the desirable properties of SpyTag/SpyCatcher in addition to other protein building blocks to develop new protein-based materials with biomedical applications. One such project involves the design of stimulus-responsive hydrogels made entirely of protein components. We took advantage of the modular nature of TPR domains, which bind C-terminal peptides, to interact with cognate peptide cross-linkers to form an ionic hydrogel network. Through the adaptation of SpyTag/SpyCatcher technology, we have developed a concatenation scheme that allows us to create branched protein topologies with multivalent peptides that correspond to TPR domains. By mixing telechelic peptide cross-linkers with their corresponding TPR arrays, we demonstrate the formation of hydrogels that can respond to a physiological stimulus. Other projects described in this text involve the development of geometric protein arrays. Such arrays have implications in signal amplification, biosensing, and enzyme scaffolding array. Using the modular, rod-like protein SasG and SpyTag/SpyCatcher technology, we were able to create discrete rectangular protein arrays with tunable dimensions. In a different project, SpyCatcher arrays were used to create complexes that can display various numbers of recognition elements on the same construct. As a proof of principle, we designed complexes that can bind to HER2, a relevant breast cancer biomarker. Finally, we were able to functionalize 2D surfaces and microcapsules using SpyTag/SpyCatcher technology and a unique, amphiphilic bacterial hydrophobin, Bs1A. Bs1A self-assembles into a stable monolayer at both air-water and water-oil interfaces. We have functionalized these proteins with SpyTag and SnoopTag for use in decorating surfaces and microcapsules with proteins of interest attached to SpyCatcher.
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