|Name||Ms. Amanda Pritzlaff|
|Organization||University of Florida|
|Topic||Biochemistry / Chem Bio.|
Galectin-3-Polymer Conjugates for Self-Assembling and Cell-Targeted Drug Delivery Vehicles
Amanda Pritzlaff, Dominic Rucco, Daniel Savin
University of Florida Chemistry Department Butler Polymer Lab
The human carbohydrate-binding lectin protein galectin-3 is upregulated in many types of cancers and is associated with progression and metastasis via its ability to extracellularly bind β-galactosides and form pentameric structures, which modulate cell migration and motility. Galectin-3 can be overexpressed and purified from E. coli and conjugated to self-assembling polymers in order to exploit the ability of galectin-3 to bind to the cancer extracellular matrix and aid in the specific targeting of polymeric drug delivery vehicles. Currently, E. coli strains BL21(DE3) PLysS and Origami B(DE3) overexpress His-tagged galectin-3. Affinity chromatography with a nickel-agarose column is used to purify galectin-3 from the cell lysate. Elution conditions such as imidazole concentration are being optimized for high-purity galectin-3. The effects of protein-polymer conjugation on properties such as galectin-3-sugar binding affinity and polymer self-assembly/stimuli responsiveness will first be assessed after successful purification and conjugation.