Professional Education

  • Doctor of Philosophy, S.U.N.Y. State University at Stony Brook (2017)
  • Bachelor of Arts and Science, University of Florida (2012)

Research & Scholarship

Current Research and Scholarly Interests

Identifying mechanisms by which the tumor microenvironment contributes to fundamental cellular signaling pathways responsible for regulating cancer stem cells' ability to self-renewal and promote tumor relapse in patients.


All Publications

  • Matrix Metalloproteinases (MMPs) as Cancer Therapeutic Targets Matrix Metalloproteinases in Health and Disease, Sculpting the Human Body Cathcart, J., Alford, V. M., Cao, J. World Scientific Publishing. 2017: 157–185
  • Targeting the Hemopexin-like Domain of Latent Matrix Metalloproteinase-9 (proMMP-9) with a Small Molecule Inhibitor Prevents the Formation of Focal Adhesion Junctions. ACS chemical biology Alford, V. M., Kamath, A., Ren, X., Kumar, K., Gan, Q., Awwa, M., Tong, M., Seeliger, M. A., Cao, J., Ojima, I., Sampson, N. S. 2017; 12 (11): 2788–2803


    A lack of target specificity has greatly hindered the success of inhibitor development against matrix metalloproteinases (MMPs) for the treatment of various cancers. The MMP catalytic domains are highly conserved, whereas the hemopexin-like domains of MMPs are unique to each family member. The hemopexin-like domain of MMP-9 enhances cancer cell migration through self-interaction and heterointeractions with cell surface proteins including CD44 and α4β1 integrin. These interactions activate EGFR-MAP kinase dependent signaling that leads to cell migration. In this work, we generated a library of compounds, based on hit molecule N-[4-(difluoromethoxy)phenyl]-2-[(4-oxo-6-propyl-1H-pyrimidin-2-yl)sulfanyl]-acetamide, that target the hemopexin-like domain of MMP-9. We identify N-(4-fluorophenyl)-4-(4-oxo-3,4,5,6,7,8-hexahydroquinazolin-2-ylthio)butanamide, 3c, as a potent lead (Kd = 320 nM) that is specific for binding to the proMMP-9 hemopexin-like domain. We demonstrate that 3c disruption of MMP-9 homodimerization prevents association of proMMP-9 with both α4β1 integrin and CD44 and results in the dissociation of EGFR. This disruption results in decreased phosphorylation of Src and its downstream target proteins focal adhesion kinase (FAK) and paxillin (PAX), which are implicated in promoting tumor cell growth, migration, and invasion. Using a chicken chorioallantoic membrane in vivo assay, we demonstrate that 500 nM 3c blocks cancer cell invasion of the basement membrane and reduces angiogenesis. In conclusion, we present a mechanism of action for 3c whereby targeting the hemopexin domain results in decreased cancer cell migration through simultaneous disruption of α4β1 integrin and EGFR signaling pathways, thereby preventing signaling bypass. Targeting through the hemopexin-like domain is a powerful approach to antimetastatic drug development.

    View details for DOI 10.1021/acschembio.7b00758

    View details for PubMedID 28945333

    View details for PubMedCentralID PMC5697452

  • A Novel Collagen Dot Assay for Monitoring Cancer Cell Migration. Methods in molecular biology (Clifton, N.J.) Alford, V. M., Roth, E., Zhang, Q., Cao, J. 2016; 1406: 181-187


    Cell migration is a critical determinant of cancer invasion and metastasis. Drugs targeting cancer cell migration have been hindered due to the lack of effective assays for monitoring cancer cell migration. Here we describe a novel method to microscopically monitor cell migration in a quantitative fashion. This assay can be used to study genes involved in cancer cell migration, as well as screening anticancer drugs that target this cellular process.

    View details for DOI 10.1007/978-1-4939-3444-7_15

    View details for PubMedID 26820955