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

Autor:	West, Savannah J
Předmět:	protein purification ligand binding tubulin thermodynamics calorimetry
Zdroj:	Theses and Dissertations.
Druh dokumentu:	Text
Popis:	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).
Databáze:	Networked Digital Library of Theses & Dissertations
Externí odkaz:	https://scholarsjunction.msstate.edu/td/4711 https://scholarsjunction.msstate.edu/cgi/viewcontent.cgi?article=5710&context=td Zobrazit plný text záznamu