Abstract
Fibroblast Growth Factor-1 (FGF-1) is a potent angiogenic agent that is released via the non-classical protein secretion pathway. Angiogenesis, the process of formation of new blood vessels, is vital to the formation of tumors, and is also responsible for tumor metastasis, as cancer cells travel from one part of the body to another through the newly formed vessels. Export of FGF-1 is based on the Cu2+ -dependent structure of multi-protein complexes, which involves the S100A13, a Ca2+ binding protein belonging to the family of S100 protein. The goal of this study is to characterize the structure of the FGF-1/S100A13 Data will be presented analyzing the interaction between FGF-1 and an S100A13 peptide that has been designed to mimic the binding region of FGF-1 on S100A13. The binding interaction was characterized using various biophysical techniques including ITC, DSC, proteolytic digestion, and multi-dimensional NMR spectroscopy. Characterization of the binding FGF-1/S100A13 interface is expected to shed light on the molecular mechanism(s) underlying the non-classical secretion of FGF-1.
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