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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.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Promotion of antibody orientation by unique noncovalent polymer-protein pairing: Structural elucidation, mechanistic analysis, and applications in immunoassays and biosensors.
Author:	Farris, Leslie Ruth.
Description:	93 p.
Notes:	Source: Dissertation Abstracts International, Volume: 72-08, Section: B, page: .
Notes:	Adviser: Melisenda McDonald.
Contained By:	Dissertation Abstracts International72-08B.
Subject:	Chemistry, Biochemistry.
Online resource:	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.
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500 $a Adviser: Melisenda McDonald.
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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.
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