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A Dock‐Derived PEDF Mimic Targeting Laminin Receptor Downregulates VEGF Receptor

Pigment epithelium derived factor (PEDF) is regarded as an exceptionally potent inhibitor of angiogenesis. Our lab and others have used PEDF as a novel prostate cancer therapy, as PEDF inhibits tumor establishment, vascularization, and alters malignant signaling. Recently, PEDF was identified as a binding partner for the cancer associated protein Laminin Receptor (LAMR1). LAMR1 overexpression is common in a variety of cancers including prostate, breast, and colon. In an attempt to mimic the protein‐protein interaction between PEDF and LAMR1, we used a structure based drug design approach. After screening 14,000 compounds in silico against the crystal structure of LAMR1 and screening 7 compounds in vitro against five cell types, we identified a hit compound with low micromolar anti‐proliferative capacity against the prostate cancer cell line PC3. Our hit compound markedly decreased VEGFR at the mRNA level, a finding that has been associated with PEDF expression. In an unbiased redock, our hit compound bound a laminin binding site on the crystal structure of LAMR1. This binding appears to be facilitated by a hydrogen bond between the compound and HIS169 of LAMR1. Next, we will confirm compound activity via a fluorescent polarization assay and endothelial tube formation.