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Predicting the physical stability of biopolymers by self-interaction chromatography

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dc.contributor.authorPayne, Robert W., author
dc.contributor.authorHenry, Charles S., advisor
dc.date.accessioned2024-03-13T20:12:29Z
dc.date.available2024-03-13T20:12:29Z
dc.date.issued2008
dc.description.abstractBiopolymers, including proteins and peptides, are increasingly taking the place of small molecules in manufacturing, health and home applications. The advantage of using biopolymers over small molecules for therapeutic applications include high activity, high specificity and low toxicity. The disadvantages of using biopolymers include large scale production, chemical instability and physical degradation. A biopolymer that shows promise for a specific application will not advance past early development if the protein lacks either chemical or physical stability. Of these two parameters, physical stability is often harder to predict and/or measure. The physical stability of a biopolymer can be improved by site-directed mutagenesis, glycosylation, post-translational modification and adjusting the solvent/co-solvent system. Quantitatively measuring the change in the physical stability of a protein in different solvent/co-solvent systems can increase the number of early developmental stage proteins that advance to commercial scale. Physical stability of proteins can be described by protein-protein interactions and measured by the osmotic second virial coefficient (B). However, current methods used to measure B such as static light scattering are not practical for large screening studies because of large protein consumption, low throughput, method variability and analyte size limitations. An alternative method to measure B is Self-Interaction Chromatography (SIC), which requires less protein, shorter analysis time, allows for miniaturization and capable of measuring B for small size biopolymer. The ability of SIC to measure B for a therapeutic protein, a peptide and membrane proteins in different solvent/co-solvent systems has been demonstrated in this dissertation.
dc.format.mediumborn digital
dc.format.mediumdoctoral dissertations
dc.identifierETDF_Payne_2008_3321301.pdf
dc.identifier.urihttps://hdl.handle.net/10217/237903
dc.languageEnglish
dc.language.isoeng
dc.publisherColorado State University. Libraries
dc.relation.ispartof2000-2019
dc.rightsCopyright and other restrictions may apply. User is responsible for compliance with all applicable laws. For information about copyright law, please see https://libguides.colostate.edu/copyright.
dc.rights.licensePer the terms of a contractual agreement, all use of this item is limited to the non-commercial use of Colorado State University and its authorized users.
dc.subjectbiopolymers
dc.subjectHPLC
dc.subjectpeptides
dc.subjectproteins
dc.subjectself-interaction chromatography
dc.subjectstability
dc.subjectanalytical chemistry
dc.titlePredicting the physical stability of biopolymers by self-interaction chromatography
dc.typeText
dcterms.rights.dplaThis Item is protected by copyright and/or related rights (https://rightsstatements.org/vocab/InC/1.0/). You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s).
thesis.degree.disciplineChemistry
thesis.degree.grantorColorado State University
thesis.degree.levelDoctoral
thesis.degree.nameDoctor of Philosophy (Ph.D.)

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