Identifying novel fibronectin binding sequences selective to strained and unstrained mechanical states
Zeller, Mark K.
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Fibronectin (Fn) is an integral protein in the Extracellular matrix (ECM) and is known for its ability to lengthen under mechanical strain. It is hypothesized that this ability is based on unfolding of the protein s tertiary structure, exposing integrin-binding domains that serve as cellular binding partners. It is through this interaction that cellular processes, such as mechanotransduction, may occur. The current methods of tracking the mechanical state of Fn is through fluorescence resonance energy transfer (FRET), which is limited to in vitro testing and is not applicable to studying Fn in tissue. It is the goal of this study to evaluate an alternative approach to tracking the mechanical unfolding of Fn. By implementing phage display, Fn fibers in relaxed and strained mechanical states were exposed to the fuse5 library to locate high affinity binders. The results produced a peptide sequence complementary to binding sites specific to the relaxed and strained states. By applying fluorophores to these high affinity binders, molecular probes can be created to quantify mechanical strain undergone by Fn in tissue.