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Imaging Prostate Cancer Microenvironment by Collagen Hybridization

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Technical Report,30 Sep 2012,29 Sep 2016

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Johns Hopkins University Baltimore United States

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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.

Subject Categories:

  • Medicine and Medical Research

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