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Chlorotoxin—A Multimodal Imaging Platform for Targeting Glioma Tumors

Chlorotoxin (CTX) is a 36-amino-acid disulfide-containing peptide derived from the venom of the scorpion Leiurus quinquestriatus. CTX alters physiology in numerous ways. It interacts with voltage gated chloride channels, Annexin-2, and matrix metalloproteinase-2 (MMP-2). CTX-based bioconjugates have...

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Autores principales: Cohen, Gadi, Burks, Scott R., Frank, Joseph A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6316809/
https://www.ncbi.nlm.nih.gov/pubmed/30486274
http://dx.doi.org/10.3390/toxins10120496
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author Cohen, Gadi
Burks, Scott R.
Frank, Joseph A.
author_facet Cohen, Gadi
Burks, Scott R.
Frank, Joseph A.
author_sort Cohen, Gadi
collection PubMed
description Chlorotoxin (CTX) is a 36-amino-acid disulfide-containing peptide derived from the venom of the scorpion Leiurus quinquestriatus. CTX alters physiology in numerous ways. It interacts with voltage gated chloride channels, Annexin-2, and matrix metalloproteinase-2 (MMP-2). CTX-based bioconjugates have been widely subjected to phase I/II clinical trials and have shown substantial promise. Many studies have demonstrated that CTX preferentially binds to neuroectodermal tumors, such as glioblastoma, without cross-reactivity to normal brain cells. With its ability to penetrate the blood-brain-barrier (BBB) and its tyrosine residue allows covalent conjugation with functional moieties, CTX is an attractive platform to explore development of diagnostic and therapeutic agents for gliomas. In this review, we outline CTX structure and its molecular targets, summarize molecular variations of CTX developed for glioma imaging, and discuss future trends and perspectives for CTX conjugates as a theranostic agent.
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spelling pubmed-63168092019-01-11 Chlorotoxin—A Multimodal Imaging Platform for Targeting Glioma Tumors Cohen, Gadi Burks, Scott R. Frank, Joseph A. Toxins (Basel) Review Chlorotoxin (CTX) is a 36-amino-acid disulfide-containing peptide derived from the venom of the scorpion Leiurus quinquestriatus. CTX alters physiology in numerous ways. It interacts with voltage gated chloride channels, Annexin-2, and matrix metalloproteinase-2 (MMP-2). CTX-based bioconjugates have been widely subjected to phase I/II clinical trials and have shown substantial promise. Many studies have demonstrated that CTX preferentially binds to neuroectodermal tumors, such as glioblastoma, without cross-reactivity to normal brain cells. With its ability to penetrate the blood-brain-barrier (BBB) and its tyrosine residue allows covalent conjugation with functional moieties, CTX is an attractive platform to explore development of diagnostic and therapeutic agents for gliomas. In this review, we outline CTX structure and its molecular targets, summarize molecular variations of CTX developed for glioma imaging, and discuss future trends and perspectives for CTX conjugates as a theranostic agent. MDPI 2018-11-26 /pmc/articles/PMC6316809/ /pubmed/30486274 http://dx.doi.org/10.3390/toxins10120496 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Cohen, Gadi
Burks, Scott R.
Frank, Joseph A.
Chlorotoxin—A Multimodal Imaging Platform for Targeting Glioma Tumors
title Chlorotoxin—A Multimodal Imaging Platform for Targeting Glioma Tumors
title_full Chlorotoxin—A Multimodal Imaging Platform for Targeting Glioma Tumors
title_fullStr Chlorotoxin—A Multimodal Imaging Platform for Targeting Glioma Tumors
title_full_unstemmed Chlorotoxin—A Multimodal Imaging Platform for Targeting Glioma Tumors
title_short Chlorotoxin—A Multimodal Imaging Platform for Targeting Glioma Tumors
title_sort chlorotoxin—a multimodal imaging platform for targeting glioma tumors
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6316809/
https://www.ncbi.nlm.nih.gov/pubmed/30486274
http://dx.doi.org/10.3390/toxins10120496
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