30th Annual Student Research Conference
Investigation of Affinity at Binding Site Between Human Epidermal Growth Factor Receptor 2 (HER2) and Herceptin
Maria Kondrashova
Dr. Bill R. Miller, Faculty Mentor
HER2 positive breast cancer results from an uncontrolled synthesis of the HER2 protein due to the amplification of the HER2 gene. Herceptin is a receptor-blocking monoclonal antibody that prevents metastasis. Many patients often develop a resistance to Herceptin. One of the mechanisms of resistance has been established as mutations on HER2 as cancer progresses. This allows the tumor cells to continue replicating. The current study investigates the binding free energies between the HER2 receptor and Herceptin to determine if the amino acid sequence can be mutated to create a stronger interaction between the HER2 receptor and the antibody. The binding free energies generated for every residue in the HER2/Herceptin complex allowed us to closely examine each residue?s contribution to binding. The third loop will be further evaluated to determine if any other residues can be mutated to strengthen the total binding affinity of the HER2/Herceptin complex.
Keywords: HER2, Herceptin, binding affinity, free binding energy
Topic(s):Chemistry
Biology
Presentation Type: Poster
Session: 7-
Location: GEO - SUB
Time: