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Benqian Wei_Master Thesis.pdf (2.52 MB)

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Characterization of supramolecular peptide-polymer bioconjugates using multistage tandem mass spectrometry

Wei, Benqian
http://orcid.org/0000-0003-4853-4848
http://rave.ohiolink.edu/etdc/view?acc_num=akron1554221356363952

Abstract Details

2019, Master of Science, University of Akron, Polymer Science.
Mass spectrometry (MS) is an essential analytical tool for the characterization of the structure of biological macromolecules, including protein-protein and protein-ligand complexes. One-dimensional MS separates gas-phase analyte ions based on their mass to charge ratio (m/z); however, to obtain more detailed structural information, tandem MS (MS/MS), which involves isolation and subsequent fragmentation of a precursor ion, is required. In this thesis, electrospray ionization multistage tandem mass spectrometry (ESI-MSn) was employed to examine the non-covalent complexes between poly(styrene sulfonate) (PSS) and poly-L-lysine (PLL). During single-stage ion activation, the PLL peptide chain mainly underwent backbone cleavages without disruption of the non-covalent interaction which could only be broken via sequential application of electron transfer dissociation (ETD) and collisionally activated dissociation (CAD), indicating strong binding interactions between the two polyelectrolyte chains. Such binding properties make PSS a potential “non-covalent (supramolecular) label” for determining the surface accessibility of basic residues on a peptide or protein. To probe this premise, non-covalent complexes of substance P and PSS were characterized by ESI-MSn using different ion activation methods. Both MS2 and MS3 experiments on the substance P + PSS complex resulted in the formation of bn (on CAD) or cn (on ETD) fragments attached non-covalently to the intact PSS chain. All peptide fragments containing the intact PSS chain included Arg1, Lys3, and Gln5, pointing out that these residues, which are located near the N-terminus, are most likely involved in the noncovalent interaction with PSS. In contrast, Gln6 was excluded from this fragment series, attesting a much weaker interaction with PSS due to lesser accessibility. The strong tendency of PSS to bind peptides noncovalently at sites that can be elucidated by MSn demonstrates a proof-of-concept for the capacity of this approach to unveil higher order structure in proteins.
Chrys Wesdemiotis (Advisor)
Toshikazu Miyoshi (Committee Member)
69 p.
Analytical Chemistry; Chemistry; Polymers

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Citations

  • Wei, B. (2019). Characterization of supramolecular peptide-polymer bioconjugates using multistage tandem mass spectrometry [Master's thesis, University of Akron]. OhioLINK Electronic Theses and Dissertations Center. http://rave.ohiolink.edu/etdc/view?acc_num=akron1554221356363952

    APA Style (7th edition)

  • Wei, Benqian. Characterization of supramolecular peptide-polymer bioconjugates using multistage tandem mass spectrometry. 2019. University of Akron, Master's thesis. OhioLINK Electronic Theses and Dissertations Center, http://rave.ohiolink.edu/etdc/view?acc_num=akron1554221356363952.

    MLA Style (8th edition)

  • Wei, Benqian. "Characterization of supramolecular peptide-polymer bioconjugates using multistage tandem mass spectrometry." Master's thesis, University of Akron, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=akron1554221356363952

    Chicago Manual of Style (17th edition)

akron1554221356363952
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This open access ETD is published by University of Akron and OhioLINK.