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Author

XIN LIFollow

Author ORCID Identifier

https://orcid.org/0000-0002-2045-9586

Document Type

Campus-Only Access for Five (5) Years

Degree Name

Doctor of Philosophy (PhD)

Degree Program

Chemistry

Year Degree Awarded

2020

Month Degree Awarded

February

First Advisor

Min Chen

Subject Categories

Analytical Chemistry | Biophysics | Biotechnology

Abstract

Membrane proteins take up about one-third of all human proteins, and they are targets for more than half of all drugs. This thesis will describe how these membrane proteins and peptides can be adapted into miniaturized devices for fundamental research as well as biotechnological applications. The Escherichia coli Cytolysin A (ClyA) is deployed as a label-free nanopore tweezer with a high temporal resolution to resolve protein dynamics at the single-molecule level in real-time. My work identified the anomeric binding modes of maltose-binding protein (MBP) for the first time, derived the kinetics and thermodynamics of the protein-substrate interactions, and shed light on the mechanism of substrate recognition by MBP. I also adapted and improved the traditional droplet-interface bilayer (DIB) techniques for quantitating cell-penetrating peptides (CPPs) assisted macromolecular trafficking. In this work, we discovered the driving force for CPP-assisted translocation and validated a DIB-based approach for high throughput screening of the efficacy of CPPs.

DOI

https://doi.org/10.7275/axyn-jc67

Creative Commons License

Creative Commons Attribution-Noncommercial 4.0 License
This work is licensed under a Creative Commons Attribution-Noncommercial-Share Alike 4.0 License.

Available for download on Monday, February 01, 2021

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