國立高雄大學圖資館 |

語系: 繁體中文

說明(常見問題)

圖資館首頁

登入

回首頁

切換: 標籤 | MARC模式 | ISBD

Promotion of antibody orientation by...

Farris, Leslie Ruth.

Promotion of antibody orientation by unique noncovalent polymer-protein pairing: Structural elucidation, mechanistic analysis, and applications in immunoassays and biosensors.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Promotion of antibody orientation by unique noncovalent polymer-protein pairing: Structural elucidation, mechanistic analysis, and applications in immunoassays and biosensors.
作者:	Farris, Leslie Ruth.
面頁冊數:	93 p.
附註:	Source: Dissertation Abstracts International, Volume: 72-08, Section: B, page: .
附註:	Adviser: Melisenda McDonald.
Contained By:	Dissertation Abstracts International72-08B.
標題:	Chemistry, Biochemistry.
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3459183
ISBN:	9781124693736

Promotion of antibody orientation by unique noncovalent polymer-protein pairing: Structural elucidation, mechanistic analysis, and applications in immunoassays and biosensors.
Farris, Leslie Ruth.

Promotion of antibody orientation by unique noncovalent polymer-protein pairing: Structural elucidation, mechanistic analysis, and applications in immunoassays and biosensors. - 93 p.

Source: Dissertation Abstracts International, Volume: 72-08, Section: B, page: .

Thesis (Ph.D.)--University of Massachusetts Lowell, 2011.

The ALYGNSA is an affinity based antibody orientation system produced through the interaction of the polymer Poly(methyl methacrylate) (PMMA) and recombinant Protein G (rProG), a Streptococcal protein. In conjunction with a PMMA surface, rProG binds with the Fc region of antibodies such that they are more frequently oriented according to earlier fluorescence assay studies. However, the underlying mechanism has yet to be determined. The objective of this work is three fold: to explore the potential for specific association of the rProG and PMMA that would improve antibody orientation, to examine the orientation of the prepared antibody bound surface, and to use this system to assess the quantitative benefit of orientation with immunoassay and biosensor applications. A tertiary structure model of the full rProG was created using the iterative threading assembly refinement (I-Tasser) server. The rProG model with the highest confidence score and short chains of PMMA were subject to docking experiments through the GPU based Hex server. A five residue section with the sequence TPATP was identified as a potential interaction site. Thus, a complete model was generated for the ternary system. Non-contact atomic force microscopy was used to examine the orientation of the ALYGNSA surface; PMMA treated with rProG, and hIgG. Height threshold grain analysis comparisons with gold nanoparticle standards yielded further evidence of orientation. Lastly, ALYGNSA immunoassays for Influenza A and an array of cancer biomarkers were developed. The cancer biomarker assays revealed significantly lower limits of detection compared with their commercially available counterparts. The Influenza A assay was also successfully transferred to a label-free interferometric biosensor with an improvement in the limit of detection.

ISBN: 9781124693736Subjects--Topical Terms:

226900
Chemistry, Biochemistry.

Promotion of antibody orientation by unique noncovalent polymer-protein pairing: Structural elucidation, mechanistic analysis, and applications in immunoassays and biosensors.
LDR:02825nmm 2200277 4500 001 309747
005 20111105132504.5
008 111212s2011 ||||||||||||||||| ||eng d
020 $a 9781124693736
035 $a (UMI)AAI3459183
035 $a AAI3459183
040 $a UMI $c UMI
100 1 $a Farris, Leslie Ruth. $3 531102
245 1 0 $a Promotion of antibody orientation by unique noncovalent polymer-protein pairing: Structural elucidation, mechanistic analysis, and applications in immunoassays and biosensors.
300 $a 93 p.
500 $a Source: Dissertation Abstracts International, Volume: 72-08, Section: B, page: .
500 $a Adviser: Melisenda McDonald.
502 $a Thesis (Ph.D.)--University of Massachusetts Lowell, 2011.
520 $a The ALYGNSA is an affinity based antibody orientation system produced through the interaction of the polymer Poly(methyl methacrylate) (PMMA) and recombinant Protein G (rProG), a Streptococcal protein. In conjunction with a PMMA surface, rProG binds with the Fc region of antibodies such that they are more frequently oriented according to earlier fluorescence assay studies. However, the underlying mechanism has yet to be determined. The objective of this work is three fold: to explore the potential for specific association of the rProG and PMMA that would improve antibody orientation, to examine the orientation of the prepared antibody bound surface, and to use this system to assess the quantitative benefit of orientation with immunoassay and biosensor applications. A tertiary structure model of the full rProG was created using the iterative threading assembly refinement (I-Tasser) server. The rProG model with the highest confidence score and short chains of PMMA were subject to docking experiments through the GPU based Hex server. A five residue section with the sequence TPATP was identified as a potential interaction site. Thus, a complete model was generated for the ternary system. Non-contact atomic force microscopy was used to examine the orientation of the ALYGNSA surface; PMMA treated with rProG, and hIgG. Height threshold grain analysis comparisons with gold nanoparticle standards yielded further evidence of orientation. Lastly, ALYGNSA immunoassays for Influenza A and an array of cancer biomarkers were developed. The cancer biomarker assays revealed significantly lower limits of detection compared with their commercially available counterparts. The Influenza A assay was also successfully transferred to a label-free interferometric biosensor with an improvement in the limit of detection.
590 $a School code: 0111.
650 4 $a Chemistry, Biochemistry. $3 226900
650 4 $a Health Sciences, Immunology. $3 226966
690 $a 0487
690 $a 0982
710 2 $a University of Massachusetts Lowell. $3 492831
773 0 $t Dissertation Abstracts International $g 72-08B.
790 1 0 $a McDonald, Melisenda, $e advisor
790 $a 0111
791 $a Ph.D.
792 $a 2011
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3459183