Breast Tumor Specific Peptides: Development of Breast Carcinoma Diagnostic and Therapeutic Agents
Abstract
This proposal describes a body of research focused on the identification and development of peptides as breast tumor imaging and therapeutic agents. Peptides that bound the breast carcinoma associated Thomsen-Friedenreich (T) antigen and erbB-2 receptor were isolated from random peptide bacteriophage display libraries. A 15 amino acid peptide (P3O) and a 6 amino acid peptide (P6.1) were shown to specifically bind T antigen and the erbB-2 extracellular domain, respectively. Both peptides bound breast carcinoma cells, but not normal human endothelial cells in vitro. The P3O peptide was shown to inhibit breast carcinoma cell homotypic aggregation and breast carcinoma endothelial cell adhesion. Tumor cell aggregation and adhesion to endothelial cells are thought to be important processes in metastasis. Inhibitors of these processes may provide important leads in the development of anti-metastatic therapeutics. Peptide 6.1 exhibited high specificity and affinity for breast cancer cells expressing erbB-2 on their surfaces. Analogs of P6. 1 will be radiolabeled and examined for their potentials as breast tumor imaging or therapeutic agents.
Document Details
- Document Type
- Technical Report
- Publication Date
- Nov 01, 1999
- Accession Number
- ADB262475
Entities
People
- Thomas P. Quinn
Organizations
- University of Missouri