자료유형  

 학위논문

Control Number  

0016934571

International Standard Book Number  

9798380470858

Dewey Decimal Classification Number  

617

Main Entry-Personal Name  

Kilgour, Katie M.

Publication, Distribution, etc. (Imprint  

[S.l.] : North Carolina State University., 2023

Publication, Distribution, etc. (Imprint  

Ann Arbor : ProQuest Dissertations & Theses, 2023

Physical Description  

1 online resource(206 p.)

General Note  

Source: Dissertations Abstracts International, Volume: 85-04, Section: B.

General Note  

Advisor: Menegatti, Stefano;Daniele, Michael;Genzer, Jan;Wei, Quinshan;Cheng, Ke.

Dissertation Note  

Thesis (Ph.D.)--North Carolina State University, 2023.

Restrictions on Access Note  

This item must not be sold to any third party vendors.

Summary, Etc.  

요약Affinity binding of proteins and peptides plays a key role in therapeutic drug dosing as well as regenerative medicine. Changes in protein binding affinity cause clinically relevant changes in the concentration of conjugated antibodies and proteins which directly affect the effectiveness of treatment. In regenerative medicine, one of the biggest challenges to maximize tissue regeneration at the site of injury has been to accurately deliver proteins in a systematic manner. Additionally, drugs, such as adalimumab, require frequent lab visits for routine blood testing to be properly dosed; however, with the lengthy process to measure drug concentration, many patients receive inaccurate doses, negatively affecting their treatment. Thus, the focus of this dissertation has been to use the binding affinity of proteins to develop: (1) a real-time method for measuring therapeutic antibodies and (2) a tissue scaffold to deliver proteins to an injured site for maximum tissue regeneration.In this dissertation, the affinity binding of proteins to antibodies has been extensively investigated to develop a method for real-time monitoring of antibody concentrations in biological fluids. Herein, an affinity complex is formed between an analyte antibody and two fluorescent affinity tags, the consequent antigen and protein L. The proximity of the affinity tags when bound to antibody results in a linear fluorescent quenching, affording the concentration of antibody to be easily measured. The dual-affinity ratiometric quenching (DARQ) can be measured from collected saliva or plasma samples in under 5 minutes, making this technique more desirable than the current standards (i.e. ELISA), which require ~5-6 hrs to complete.Additionally, a tissue scaffold modified with peptides is used to pattern proteins in a non-covalent manner that affords easy uptake by resident cells. The developed scaffold introduces functionalization of gelatin methacryloyl (GelMA) with peptides that have specific binding affinity to growth factors, namely, vascular endothelial growth factor (VEGF), erythropoietin (EPO), and angiopoietin-1 (ANG1). The specific binding of the growth factors to the respective peptide allows for spatial patterning and release of the proteins, inducing controlled cell behavior. The scaffold affords a method to control protein delivery to resident cells, in turn, giving the ability to better control tissue regeneration compared to previous studies.

Subject Added Entry-Topical Term  

Tissue engineering.

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Monoclonal antibodies.

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Vascular endothelial growth factor.

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Severe acute respiratory syndrome coronavirus 2.

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Rheumatoid arthritis.

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Sensors.

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Diagnostic tests.

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Labeling.

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Biomedical materials.

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Energy.

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Chromatography.

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Antigens.

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Enzymes.

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Reproducibility.

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Cell culture.

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Hydrogels.

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Angiogenesis.

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COVID-19.

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Competition.

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Biomedical engineering.

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Cellular biology.

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Immunology.

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Materials science.

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Medicine.

Added Entry-Corporate Name  

North Carolina State University.

Host Item Entry  

Dissertations Abstracts International. 85-04B.

Host Item Entry  

Dissertation Abstract International

Electronic Location and Access  

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Control Number  

joongbu:642324