STTR Phase I: Protease-based purification of recombinant human matrix metalloproteases

The broader impact of this Small Business Technology Transfer (STTR) Phase I project is an enabling technology to improve research into many diseases. This STTR project will develop human matrix metalloprotease (MMPs), a class of enzymes that degrade many biomolecules including collagen, the most abundant structural protein in the human body. MMPs are critical for numerous normal and pathological processes, such as tumor growth.

However, MMPs are expensive to produce, and researchers need a reliable source of well-characterized human MMPs so that researchers can pursue high quality, reliable experiments on basic science and medical applications. Furthermore, this project can impact other fields that use enzymes, such as the food industry, renewable energy, and human health.

The proposed project will commercialize inexpensive recombinant human MMPs produced in E. coli. MMPs degrade and regulate various structural components of the extracellular matrix (ECM), impacting pathologies such as metastasis of solid tumors, which cannot occur without MMP-mediated degradation of collagens. Recombinant MMPs can support this research.

This STTR project will advance development of protease-based protein purification without chromatography, enabling rapid and low-cost purification. The technical R&D tasks include developing technical assessments for MMPs. The technical assessments will contain raw and curated data for purity, identity, concentration, and activity of MMPs at different solution conditions.

This project will investigate development of MMPs as anti-biofilm and anti-clot agents beyond the traditional collagen degradation field of research. The protease-based method used to obtain MMPs can be used to purify other proteins as well. MMPs also have biotechnological applications in broad-spectrum degradation of tissue components for cell isolation from tissue samples and diseases involving aberrant collagen depositions.

This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.