Thermodynamic Studies of the Binding of RPC2, ([Ru(Ph₂phen)₃]²⁺), to Purified Tubulin and Microtubules

Author

Savannah J. West

Issuing Body

Mississippi State University

Advisor

Lewis, Edwin A.

Committee Member

Emerson, Joseph

Committee Member

Fitzkee, Nick

Date of Degree

5-3-2019

Document Type

Graduate Thesis - Open Access

Major

Chemistry

Degree Name

Master of Science

College

College of Arts and Sciences

Department

Department of Chemistry

Abstract

Tubulin and elastin-like polypeptides (ELPs) both form large protein structures which can be thermodynamically evaluated using isothermal titration calorimetry and differential scanning calorimetry. ELPs are thermos-responsive biopolymers that undergo phase separation and form coacervates when heated. This project assesses the liquid-liquid phase separation of an ELP sequence derived from tropoelastin with a SynB1 cell-penetrating peptide attached to the N-terminus in conjunction with the chemotherapeutic drug doxorubicin. Microtubules (MTs) are a dynamic cellular structure formed of tubulin alpha/beta-heterodimers and are responsible for several important cellular processes, making them a viable target for anti-cancer drugs. There has been extensive research done to identify new ligands that show selective binding to microtubules. Ruthenium (II) polypyridyl complexes (RPCs) have been found to promote the polymerization of tubulin into microtubules. ITC has been used to determine the binding affinity of [Ru(II)(Ph2phen)3]2+ (RPC2).

URI

https://hdl.handle.net/11668/21170

Recommended Citation

West, Savannah J., "Thermodynamic Studies of the Binding of RPC2, ([Ru(Ph₂phen)₃]²⁺), to Purified Tubulin and Microtubules" (2019). Theses and Dissertations. 4711.
https://scholarsjunction.msstate.edu/td/4711