Gadolinium tagged osteoprotegerin-mimicking peptide : a novel magnetic resonance imaging biospecific contrast agent for the inhibition of osteoclastogenesis and osteoclast activity

Mbundi, Lubinda, Meikle, Steve T., Busquets, Rosa, Dowell, Nicholas G., Cercignani, Mara and Santin, Matteo (2018) Gadolinium tagged osteoprotegerin-mimicking peptide : a novel magnetic resonance imaging biospecific contrast agent for the inhibition of osteoclastogenesis and osteoclast activity. Nanomaterials, 8(6), p. 399. ISSN (online) 2079-4991

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Abstract

The control of osteoblast/osteoclast cross-talk is crucial in the bone remodelling process and provides a target mechanism in the development of drugs for bone metabolic diseases. Osteoprotegerin is a key molecule in this biosignalling pathway as it inhibits osteoclastogenesis and osteoclast activation to prevent run-away bone resorption. This work reports the synthesis of a known osteoprotegerin peptide analogue, YCEIEFCYLIR (OP3-4), and its tagging with a gadolinium chelate, a standard contrast agent for magnetic resonance imaging. The resulting contrast agent allows the simultaneous imaging and treatment of metabolic bone diseases. The gadolinium-tagged peptide was successfully synthesised, showing unaltered magnetic resonance imaging contrast agent properties, a lack of cytotoxicity, and dose-dependent inhibition of osteoclastogenesis in vitro. These findings pave the way toward the development of biospecific and bioactive contrast agents for the early diagnosis, treatment, and follow up of metabolic bone diseases such as osteoporosis and osteosarcoma.

Item Type: Article
Uncontrolled Keywords: osteoclastogenesis, RANK-RANKL-OPG, mimetic peptide, Gadolinium chelate, MRI
Research Area: Biological sciences
Chemistry
Faculty, School or Research Centre: Faculty of Science, Engineering and Computing (until 2017) > School of Pharmacy and Chemistry
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Depositing User: Rosa Busquets
Date Deposited: 11 Jun 2018 09:09
Last Modified: 13 Jul 2018 13:29
DOI: https://doi.org/10.3390/nano8060399
URI: http://eprints.kingston.ac.uk/id/eprint/41188

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