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Med Oncol. 2017 Oct 6;34(11):184. doi: 10.1007/s12032-017-1042-y.

Toward a new and noninvasive diagnostic method of papillary thyroid cancer by using peptide vectorized contrast agents targeted to galectin-1.

Author information

1
Department of General, Organic and Biomedical Chemistry, University of Mons, Avenue Victor Maistriau 19, 7000, Mons, Belgium.
2
Laboratory for Chemistry of Novel Materials, Center for Innovation in Materials and Polymers, University of Mons, Avenue Victor Maistriau, 19, 7000, Mons, Belgium.
3
Department of Pathology, Erasme Hospital, Université Libre de Bruxelles, Route de Lennik 808, 1070, Brussels, Belgium.
4
DIAPath, Center for Microscopy and Molecular Imaging, Rue Adrienne Bolland, 8, 6041, Charleroi, Belgium.
5
Center for Microscopy and Molecular Imaging, Rue Adrienne Bolland, 8, 6041, Charleroi, Belgium.
6
Laboratory of Human Anatomy and Experimental Oncology, University of Mons, Avenue du Champ de Mars, 6, 7000, Mons, Belgium.
7
Department of General, Organic and Biomedical Chemistry, University of Mons, Avenue Victor Maistriau 19, 7000, Mons, Belgium. carmen.burtea@umons.ac.be.

Abstract

The incidence of papillary thyroid cancer has increased these last decades due to a better detection. High prevalence of nodules combined with the low incidence of thyroid cancers constitutes an important diagnostic challenge. We propose to develop an alternative diagnostic method to reduce the number of useless and painful thyroidectomies using a vectorized contrast agent for magnetic resonance imaging. Galectin-1 (gal-1), a protein overexpressed in well-differentiated thyroid cancer, has been targeted with a randomized linear 12-mer peptide library using the phage display technique. Selected peptides have been conjugated to ultrasmall superparamagnetic particles of iron oxide (USPIO). Peptides and their corresponding contrast agents have been tested in vitro for their specific binding and toxicity. Two peptides (P1 and P7) were selected according to their affinity toward gal-1. Their binding has been revealed by immunohistochemistry on human thyroid cancer biopsies, and they were co-localized with gal-1 by immunofluorescence on TPC-1 cell line. Both peptides induce a decrease in TPC-1 cells' adhesion to gal-1 immobilized on culture plates. After coupling to USPIO, the peptides preserved their affinity toward gal-1. Their specific binding has been corroborated by co-localization with gal-1 expressed by TPC-1 cells and by their ability to compete with anti-gal-1 antibody. The peptides and their USPIO derivatives produce no toxicity in HepaRG cells as determined by MTT assay. The vectorized contrast agents are potential imaging probes for thyroid cancer diagnosis. Moreover, the two gal-1-targeted peptides prevent cancer cell adhesion by interacting with the carbohydrate-recognition domain of gal-1.

KEYWORDS:

Diagnosis; Galectin-1; Peptides; Phage display; Thyroid cancer; Ultrasmall superparamagnetic particles of iron oxide

PMID:
28986753
DOI:
10.1007/s12032-017-1042-y
[Indexed for MEDLINE]

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