東華大學圖書館 |

Language: English

Help

回圖書館首頁

手機版館藏查詢

Back

Switch To: Labeled | MARC Mode | ISBD

A new method for designing protein-b...

Sandros, Marinella G.

Linked to FindBook

Google Book

Amazon

博客來

A new method for designing protein-based reagentless nanobiosensors.

Record Type:	Electronic resources : Monograph/item
Title/Author:	A new method for designing protein-based reagentless nanobiosensors./
Author:	Sandros, Marinella G.
Description:	202 p.
Notes:	Source: Dissertation Abstracts International, Volume: 67-05, Section: B, page: 2549.
Contained By:	Dissertation Abstracts International67-05B.
Subject:	Chemistry, Biochemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3211016
ISBN:	9780542702105

A new method for designing protein-based reagentless nanobiosensors.
Sandros, Marinella G.

A new method for designing protein-based reagentless nanobiosensors. - 202 p.

Source: Dissertation Abstracts International, Volume: 67-05, Section: B, page: 2549.

Thesis (Ph.D.)--Wayne State University, 2006.

A biosensor is a device that contains a biomolecule in close proximity to an electronic device. The function of a biosensor is to produce a digital electronic signal that is proportional to the analyte being detected in solution. A biosensor offers superior selectivity for analyte detection than typical chemical sensors. A general method for designing self-contained protein-based fluorescent biosensors will be developed. This new biosensing tool will be able to measure reliably a wide range of analytes for medical applications, environmental analysis, food analysis, and homeland security. Typical fluorescent-based biosensors employ organic dyes for analyte detection. Organic dyes suffer from low stability after illumination and weak signal intensity. Semiconducting nanoparticles are excellent fluorescent probes compared to organic dyes because these probes are extremely bright and offer better stability. Proteins are known to bind specifically to a wide range of analytes. By integrating analyte-induced structural rearrangement of proteins to an extremely bright and stable fluorophore, highly selective, reversible and robust biosensors will be produced. To generate a self-contained biosensor, the reporter molecule must be attached to the biomolecule and no additional reagents are introduced other than the analyte. Analyte-induced structural rearrangements in proteins result with 1--5 A change in atom positions. Electron transfer is a sensitive detection method for detecting small atomic movements. Therefore, analyte-induced changes in electron transfer quenching of nanoparticle fluorescence can be mediated by a protein and should produce a self-contained biosensor. Self-contained biosensors were developed in this thesis by attaching a redox active ruthenium complex to a surface cysteine on maltose binding protein that was fused to metallothionein (MBP-MT). This metal containing protein is adsorbed to water soluble CdSe or CdSe ZnS nanoparticles. These metal complex modified MBP-MT/nanoparticle assemblies demonstrate maltose (analyte)-dependent changes in nanoparticle emission intensities, which are controlled by electron transfer. In this work, MBP was used as a prototype. Structurally similar proteins can now be swapped with MBP to generate biosensors for other analytes. Apart from being able to detect a wide range of analytes, these biosensors are highly reproducible, selective, and reversible.

ISBN: 9780542702105Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

A new method for designing protein-based reagentless nanobiosensors.
LDR:03318nmm 2200277 4500 001 1831863
005 20070529074737.5
008 130610s2006 eng d
020 $a 9780542702105
035 $a (UnM)AAI3211016
035 $a AAI3211016
040 $a UnM $c UnM
100 1 $a Sandros, Marinella G. $3 1920627
245 1 2 $a A new method for designing protein-based reagentless nanobiosensors.
300 $a 202 p.
500 $a Source: Dissertation Abstracts International, Volume: 67-05, Section: B, page: 2549.
500 $a Adviser: David E. Benson.
502 $a Thesis (Ph.D.)--Wayne State University, 2006.
520 $a A biosensor is a device that contains a biomolecule in close proximity to an electronic device. The function of a biosensor is to produce a digital electronic signal that is proportional to the analyte being detected in solution. A biosensor offers superior selectivity for analyte detection than typical chemical sensors. A general method for designing self-contained protein-based fluorescent biosensors will be developed. This new biosensing tool will be able to measure reliably a wide range of analytes for medical applications, environmental analysis, food analysis, and homeland security. Typical fluorescent-based biosensors employ organic dyes for analyte detection. Organic dyes suffer from low stability after illumination and weak signal intensity. Semiconducting nanoparticles are excellent fluorescent probes compared to organic dyes because these probes are extremely bright and offer better stability. Proteins are known to bind specifically to a wide range of analytes. By integrating analyte-induced structural rearrangement of proteins to an extremely bright and stable fluorophore, highly selective, reversible and robust biosensors will be produced. To generate a self-contained biosensor, the reporter molecule must be attached to the biomolecule and no additional reagents are introduced other than the analyte. Analyte-induced structural rearrangements in proteins result with 1--5 A change in atom positions. Electron transfer is a sensitive detection method for detecting small atomic movements. Therefore, analyte-induced changes in electron transfer quenching of nanoparticle fluorescence can be mediated by a protein and should produce a self-contained biosensor. Self-contained biosensors were developed in this thesis by attaching a redox active ruthenium complex to a surface cysteine on maltose binding protein that was fused to metallothionein (MBP-MT). This metal containing protein is adsorbed to water soluble CdSe or CdSe ZnS nanoparticles. These metal complex modified MBP-MT/nanoparticle assemblies demonstrate maltose (analyte)-dependent changes in nanoparticle emission intensities, which are controlled by electron transfer. In this work, MBP was used as a prototype. Structurally similar proteins can now be swapped with MBP to generate biosensors for other analytes. Apart from being able to detect a wide range of analytes, these biosensors are highly reproducible, selective, and reversible.
590 $a School code: 0254.
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Chemistry, Inorganic. $3 517253
690 $a 0487
690 $a 0488
710 2 0 $a Wayne State University. $3 975058
773 0 $t Dissertation Abstracts International $g 67-05B.
790 1 0 $a Benson, David E., $e advisor
790 $a 0254
791 $a Ph.D.
792 $a 2006
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3211016