Characterization of polymers and supramolecular protein-polymer bioconjugates using mass spectrometry

Bibliographic Details
Main Author: Gao, Yuan
Language:English
Published: University of Akron / OhioLINK 2021
Subjects:
Online Access:http://rave.ohiolink.edu/etdc/view?acc_num=akron1619735971168192
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spelling ndltd-OhioLink-oai-etd.ohiolink.edu-akron16197359711681922021-08-03T07:17:18Z Characterization of polymers and supramolecular protein-polymer bioconjugates using mass spectrometry Gao, Yuan Polymers Mass Spectrometry Polymer Protein-Polymer Bioconjugates Mass spectrometry (MS) is increasingly used for the characterization of polymers and supramolecular protein-polymer bioconjugates; especially after the introduction of soft ionization methods such as electrospray ionization (ESI) and matrix-assisted laser desorption/ionization (MALDI). Regular MS measures molecular weight information by detecting the mass-to-charge (m/z) ratio. However, if analyzing the structure of a complicated molecule such as a protein-polymer bioconjugate, information besides the molecular mass is necessary. Tandem MS (MS/MS), which involves isolation and fragmentation of a precursor ion, is widely used to gain more detailed structural information. MALDI-MS is a powerful technique for the analysis of polymers. One of the most important steps for MALDI analysis is sample preparation. MALDI sample preparation aims of producing densely packed microcrystals that improve mass accuracy, resolution, and shot-to-shot reproducibility as compared to large crystals. This thesis compared three common sample preparation methods for MALDI analysis: Dried droplet, solvent-free MALDI (SF-MALDI), and surface-layer MALDI (SL-MALDI). Additionally, ESI-MS and ESI-MS/MS were used to characterize supramolecular protein-polymer bioconjugates. Acidic polymers such as poly(styrene sulfonate) (PSS) were used to form non-covalent complexes with ubiquitin, a protein with many basic amino acid binding sites. Based on studies with simple peptides, MS/MS fragmentation of the ubiquitin complexes should cause cleavages in the protein backbone but preserve the non-covalent interaction. This study will apply a method to determine the attachment site of the polymer, which would reveal the surface-accessible basic amino acid residues and the higher-order structure of ubiquitin. 2021-04-30 English text University of Akron / OhioLINK http://rave.ohiolink.edu/etdc/view?acc_num=akron1619735971168192 http://rave.ohiolink.edu/etdc/view?acc_num=akron1619735971168192 restricted--full text unavailable until 2022-05-09 This thesis or dissertation is protected by copyright: all rights reserved. It may not be copied or redistributed beyond the terms of applicable copyright laws.
collection NDLTD
language English
sources NDLTD
topic Polymers
Mass Spectrometry
Polymer
Protein-Polymer Bioconjugates
spellingShingle Polymers
Mass Spectrometry
Polymer
Protein-Polymer Bioconjugates
Gao, Yuan
Characterization of polymers and supramolecular protein-polymer bioconjugates using mass spectrometry
author Gao, Yuan
author_facet Gao, Yuan
author_sort Gao, Yuan
title Characterization of polymers and supramolecular protein-polymer bioconjugates using mass spectrometry
title_short Characterization of polymers and supramolecular protein-polymer bioconjugates using mass spectrometry
title_full Characterization of polymers and supramolecular protein-polymer bioconjugates using mass spectrometry
title_fullStr Characterization of polymers and supramolecular protein-polymer bioconjugates using mass spectrometry
title_full_unstemmed Characterization of polymers and supramolecular protein-polymer bioconjugates using mass spectrometry
title_sort characterization of polymers and supramolecular protein-polymer bioconjugates using mass spectrometry
publisher University of Akron / OhioLINK
publishDate 2021
url http://rave.ohiolink.edu/etdc/view?acc_num=akron1619735971168192
work_keys_str_mv AT gaoyuan characterizationofpolymersandsupramolecularproteinpolymerbioconjugatesusingmassspectrometry
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