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Abstract
Background: Research in the field of antitumor chemotherapeutics pursues a key issue, drug selectivity for cancer cells. In the last 20 years, a group of proteins has attracted scientific interest as cancer chemotherapeutics due to their ability to specifically kill cancer cells while leaving normal cells undamaged. One of these proteins is apoptin.
Methods: In this study, the recent available literature regarding cell death mechanisms induced by apoptin has been reviewed. Delivering this drug to tumor cells is a challenge because it spontaneously forms soluble non-covalent aggregates. This led us to include in this review the different approaches for obtaining the maximum efficiency of apoptin entry to cancer cells.
Results: This review provides an up-to-date summary of the mechanisms by which apoptin induces selective apoptosis in tumor cells while leaving normal cells undamaged. It highlights the relationship between the apoptosis mechanism induced by this protein and its functional motifs. Apoptin has been described as an intrinsically disordered protein, which explains its ability to interact with multiple partners and affect multiple pathways inside the cell. Characterization of the different partners and pathways induced by apoptin has begun to shed light on the molecular basis of apoptin’s tumor-selective cytotoxicity.
Conclusion: The findings confirm the interest in apoptin as a potentially safe antitumor drug. Research still needed to be conducted to find an effective way to deliver apoptin for use in clinics.
Keywords: Apoptin, cancer, viral protein, DNA damage response, apoptosis, antitumor drug.
Current Medicinal Chemistry
Title:Apoptin, A Versatile Protein with Selective Antitumor Activity
Volume: 25 Issue: 30
Author(s): Jessica Castro, Marc Ribo, Antoni Benito*Maria Vilanova*
Affiliation:
- Laboratori d`Enginyeria de Proteines, Departament de Biologia, Facultat de Ciencies, Universitat de Girona, Campus de Montilivi, Maria Aurelia Capmany 40, 17003, Girona,Spain
- Laboratori d`Enginyeria de Proteines, Departament de Biologia, Facultat de Ciencies, Universitat de Girona, Campus de Montilivi, Maria Aurelia Capmany 40, 17003, Girona,Spain
Keywords: Apoptin, cancer, viral protein, DNA damage response, apoptosis, antitumor drug.
Abstract: Background: Research in the field of antitumor chemotherapeutics pursues a key issue, drug selectivity for cancer cells. In the last 20 years, a group of proteins has attracted scientific interest as cancer chemotherapeutics due to their ability to specifically kill cancer cells while leaving normal cells undamaged. One of these proteins is apoptin.
Methods: In this study, the recent available literature regarding cell death mechanisms induced by apoptin has been reviewed. Delivering this drug to tumor cells is a challenge because it spontaneously forms soluble non-covalent aggregates. This led us to include in this review the different approaches for obtaining the maximum efficiency of apoptin entry to cancer cells.
Results: This review provides an up-to-date summary of the mechanisms by which apoptin induces selective apoptosis in tumor cells while leaving normal cells undamaged. It highlights the relationship between the apoptosis mechanism induced by this protein and its functional motifs. Apoptin has been described as an intrinsically disordered protein, which explains its ability to interact with multiple partners and affect multiple pathways inside the cell. Characterization of the different partners and pathways induced by apoptin has begun to shed light on the molecular basis of apoptin’s tumor-selective cytotoxicity.
Conclusion: The findings confirm the interest in apoptin as a potentially safe antitumor drug. Research still needed to be conducted to find an effective way to deliver apoptin for use in clinics.
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Cite this article as:
Castro Jessica, Ribo Marc, Benito Antoni*, Vilanova Maria*, Apoptin, A Versatile Protein with Selective Antitumor Activity, Current Medicinal Chemistry 2018; 25 (30) . https://dx.doi.org/10.2174/0929867325666180309112023
DOI https://dx.doi.org/10.2174/0929867325666180309112023 |
Print ISSN 0929-8673 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-533X |
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