東華大學圖書館 |

語系: 繁體中文

說明(常見問題)

回圖書館首頁

手機版館藏查詢

登入

回首頁

切換: 標籤 | MARC模式 | ISBD

Elastin-Like Polypeptide Fusion Tag ...

Johnson, Tamina L.

FindBook

Google Book

Amazon

博客來

Elastin-Like Polypeptide Fusion Tag as a Protein-Dependent Solubility Enhancer of Cysteine-Knot Growth Factors.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Elastin-Like Polypeptide Fusion Tag as a Protein-Dependent Solubility Enhancer of Cysteine-Knot Growth Factors./
作者:	Johnson, Tamina L.
出版者:	Ann Arbor : ProQuest Dissertations & Theses, : 2018,
面頁冊數:	123 p.
附註:	Source: Dissertations Abstracts International, Volume: 79-12, Section: B.
Contained By:	Dissertations Abstracts International79-12B.
標題:	Molecular biology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10787317
ISBN:	9780355982763

Elastin-Like Polypeptide Fusion Tag as a Protein-Dependent Solubility Enhancer of Cysteine-Knot Growth Factors.
Johnson, Tamina L.

Elastin-Like Polypeptide Fusion Tag as a Protein-Dependent Solubility Enhancer of Cysteine-Knot Growth Factors. - Ann Arbor : ProQuest Dissertations & Theses, 2018 - 123 p.

Source: Dissertations Abstracts International, Volume: 79-12, Section: B.

Thesis (Ph.D.)--University of South Florida, 2018.

This item is not available from ProQuest Dissertations & Theses.

Elastin-like peptide (ELP) fusions promote therapeutic delivery and efficacy. Recombinant proteins, like neurotrophins, lack bioavailability, have short in vivo half-lives, and require high manufacturing costs. Fusing recombinant proteins with genetically encodable ELPs will increase bioavailability, enhance in vivo solubilization, as well as provide a cost-effective method for purification without the need for chromatography. During expression of neurotrophin-ELP (N-ELP) fusions, dense water-insoluble aggregates known as inclusion bodies (IBs) are formed. Inclusion bodies are partially and misfolded proteins that usually require denaturants like Urea for solubilization. Strong denaturants arrest ELPs stimuli-responsive property and increase unwanted aggregation, making purification difficult, yet possible. The current field of study exhibit issues with protein recovery due to solubility issues and aggregation. This study examines the solubility challenges of inclusion body proteins and the role ELP fusion tags play on IBs solubility. Elastin-like peptides are a class of stimuli-responsive biopolymers whose biocompatibility and limited toxicity are attractive for biological applications. ELPs are tunable polymers, which consist of peptide repeat units (VPGXG), where X is any amino acid except Proline while the guest residue or length of the sequence can be chosen. ELPs have uniquely tunable phase transitioning properties that allow the protein to undergo molecular self-assemblies into different nanostructures in response to the changes in their environment (e.g. pH or temperature). Optimizing the purification process via suppressing aggregation during the refolding process has increased protein recovery slightly however, more work is needed to attain 90 percent recovery. Usage of ELPs has increased the solubility of N-ELP fusions, specifically for brain-derived neurotrophic factor ELP fusions.

ISBN: 9780355982763Subjects--Topical Terms:

517296
Molecular biology.
Subjects--Index Terms:

Cysteine-knot growth factor

Elastin-Like Polypeptide Fusion Tag as a Protein-Dependent Solubility Enhancer of Cysteine-Knot Growth Factors.
LDR:03346nmm a2200421 4500 001 2267877
005 20200810100149.5
008 220629s2018 ||||||||||||||||| ||eng d
020 $a 9780355982763
035 $a (MiAaPQ)AAI10787317
035 $a (MiAaPQ)usf:14716
035 $a AAI10787317
040 $a MiAaPQ $c MiAaPQ
100 1 $a Johnson, Tamina L. $3 3545132
245 1 0 $a Elastin-Like Polypeptide Fusion Tag as a Protein-Dependent Solubility Enhancer of Cysteine-Knot Growth Factors.
260 1 $a Ann Arbor : $b ProQuest Dissertations & Theses, $c 2018
300 $a 123 p.
500 $a Source: Dissertations Abstracts International, Volume: 79-12, Section: B.
500 $a Publisher info.: Dissertation/Thesis.
500 $a Advisor: Koria, Piyush.
502 $a Thesis (Ph.D.)--University of South Florida, 2018.
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 Elastin-like peptide (ELP) fusions promote therapeutic delivery and efficacy. Recombinant proteins, like neurotrophins, lack bioavailability, have short in vivo half-lives, and require high manufacturing costs. Fusing recombinant proteins with genetically encodable ELPs will increase bioavailability, enhance in vivo solubilization, as well as provide a cost-effective method for purification without the need for chromatography. During expression of neurotrophin-ELP (N-ELP) fusions, dense water-insoluble aggregates known as inclusion bodies (IBs) are formed. Inclusion bodies are partially and misfolded proteins that usually require denaturants like Urea for solubilization. Strong denaturants arrest ELPs stimuli-responsive property and increase unwanted aggregation, making purification difficult, yet possible. The current field of study exhibit issues with protein recovery due to solubility issues and aggregation. This study examines the solubility challenges of inclusion body proteins and the role ELP fusion tags play on IBs solubility. Elastin-like peptides are a class of stimuli-responsive biopolymers whose biocompatibility and limited toxicity are attractive for biological applications. ELPs are tunable polymers, which consist of peptide repeat units (VPGXG), where X is any amino acid except Proline while the guest residue or length of the sequence can be chosen. ELPs have uniquely tunable phase transitioning properties that allow the protein to undergo molecular self-assemblies into different nanostructures in response to the changes in their environment (e.g. pH or temperature). Optimizing the purification process via suppressing aggregation during the refolding process has increased protein recovery slightly however, more work is needed to attain 90 percent recovery. Usage of ELPs has increased the solubility of N-ELP fusions, specifically for brain-derived neurotrophic factor ELP fusions.
590 $a School code: 0206.
650 4 $a Molecular biology. $3 517296
650 4 $a Polymer chemistry. $3 3173488
650 4 $a Biomedical engineering. $3 535387
653 $a Cysteine-knot growth factor
653 $a Denaturant
653 $a Elastin-like polypeptide
653 $a Inclusion body
653 $a Inverse transition cycling
653 $a Neurotrophin
690 $a 0307
690 $a 0495
690 $a 0541
710 2 $a University of South Florida. $b Chemical Engineering. $3 1685195
773 0 $t Dissertations Abstracts International $g 79-12B.
790 $a 0206
791 $a Ph.D.
792 $a 2018
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10787317