The local concentration of the extracellular matrix (ECM) proteins collagen and fibronectin that are secreted and co-localized during early development is an essential parameter regulating tissue genesis. While past studies have suggested a co-dependence of both proteins during development, where the absence of one inhibits the growth of the other, the mechanism potentiating this relationship remains largely unknown. We attempt to better understand this relationship by observing the interaction between these proteins first in solutions then when assembled as fibrils. Specifically, we ask whether collagen unfolds fibronectin, if collagen and fibronectin bind in solution, and how fibronectin alters collagen assembly kinetics. Fluorescence spectroscopy, turbidity assays, and Fourier Transform Infrared Spectroscopy were employed to observe the interactions between these proteins as they undergo fibrillogenesis. Our results suggest a co-dependency between collagen and fibronectin <i>in situ </i>that impacts fibrillogenesis in a process that can potentially be used for future tissue engineering applications.

Elucidating the co-dependence of collagen and fibronectin during fibrillogenesis

256th National Meeting (2018)

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