Single-Molecule Studies of Proteins at Polymer based Chromatographic Interfaces

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dc.contributor.advisorLandes, Christy F
dc.creatorMoringo, Nicholas A
dc.date.accessioned2020-01-14T19:35:17Z
dc.date.available2020-01-14T19:35:17Z
dc.date.created2020-05
dc.date.issued2020-01-14
dc.date.submittedMay 2020
dc.date.updated2020-01-14T19:35:17Z
dc.description.abstractThe worldwide pharmaceutical landscape has witnessed a large influx of biological-based therapeutics, termed ‘biologics’, for the successful treatment of diseases and illnesses. The downstream separation and purification of promising biologics via chromatography dominates the total production cost leading to market entry. A mechanistic examination of protein interactions at the interface of stationary phase materials can improve and enable predictive chromatographic separation optimization. Single-molecule imaging techniques, inspired by the advances of super-resolution microscopy, can capture the highly dynamic interactions of proteins at stationary phase materials. It is observed that nanoscale protein dynamics can explain experimentally observed increases in separation efficiencies. We uncover how the suppression of anomalous surface diffusion, which leads to improved separations, can be tuned with stationary phase surface chemistries, polymer packing, and ionic salt conditions. Overall, we have shown that single-molecule imaging can relate protein dynamics at the nanoscale to improved protein separations at the interface of synthetic polymer materials.
dc.format.mimetypeapplication/pdf
dc.identifier.citationMoringo, Nicholas A. "Single-Molecule Studies of Proteins at Polymer based Chromatographic Interfaces." (2020) Diss., Rice University. <a href="https://hdl.handle.net/1911/107967">https://hdl.handle.net/1911/107967</a>.
dc.identifier.urihttps://hdl.handle.net/1911/107967
dc.language.isoeng
dc.rightsCopyright is held by the author, unless otherwise indicated. Permission to reuse, publish, or reproduce the work beyond the bounds of fair use or other exemptions to copyright law must be obtained from the copyright holder.
dc.subjectsingle-molecule microscopy
dc.subjectchromatography
dc.titleSingle-Molecule Studies of Proteins at Polymer based Chromatographic Interfaces
dc.typeThesis
dc.type.materialText
thesis.degree.departmentChemistry
thesis.degree.disciplineNatural Sciences
thesis.degree.grantorRice University
thesis.degree.levelDoctoral
thesis.degree.nameDoctor of Philosophy
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