Imaging Prostate Cancer Microenvironment by Collagen Hybridization
Abstract
Small collagen mimetic peptide (CMPs) that mimic the amino acid sequence and three dimensional structure of collagen were shown to have specific binding affinity to type I collagen fibers in vitro and specifically to articular cartilage in vivo. Although the exact mechanism of binding is not known fully, evidence is accumulating that supports the idea that the CMP is binding to partially denatured domains of natural collagen by triple helical hybridization. Here we have tested CMP as a collagen targeting agent to allow imaging of stromal collagens in prostate cancer (PCa). Since CMP binds to unstructured collagen domains more readily, it is expected to exhibit selective affinity to metastatic PCa known to contain processed and denatured collagens. We employed both fluorescent and radiolabeled CMP analogs to image murine models of PCa.
Document Details
- Document Type
- Technical Report
- Publication Date
- Dec 01, 2016
- Accession Number
- AD1034746
Entities
People
- Martin G. Pomper
Organizations
- Johns Hopkins University