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Caged noble metals : Encapsulation of a cytotoxic platinum(II)-gold(I) compound within the ferritin nanocage

Ferraro, Giarita ; Petruk, Ganna LU orcid ; Maiore, Laura ; Pane, Francesca ; Amoresano, Angela ; Cinellu, Maria Agostina ; Monti, Daria Maria and Merlino, Antonello (2018) In International Journal of Biological Macromolecules 115. p.1116-1121
Abstract

The encapsulation of Pt and Au-based anticancer agents within a protein cage is a promising way to enhance the selectivity of these potential drugs. Here a cytotoxic organometallic compound containing platinum(II) and gold(I) has been encapsulated within a ferritin nanocage (AFt). Inductively plasma coupled mass spectrometry data, collected to evaluate the amount of Pt and Au within the cage, indicate disruption of the starting heterobimetallic complex upon encapsulation within the nanocage. The drug-loaded protein (Pt(II)/Au(I)-AFt) has been characterized by UV–Vis spectroscopy, circular dichroism and X-ray diffraction analysis. Data indicate that the protein maintains its fold upon encapsulation of the metallodrug and that Au(I) and... (More)

The encapsulation of Pt and Au-based anticancer agents within a protein cage is a promising way to enhance the selectivity of these potential drugs. Here a cytotoxic organometallic compound containing platinum(II) and gold(I) has been encapsulated within a ferritin nanocage (AFt). Inductively plasma coupled mass spectrometry data, collected to evaluate the amount of Pt and Au within the cage, indicate disruption of the starting heterobimetallic complex upon encapsulation within the nanocage. The drug-loaded protein (Pt(II)/Au(I)-AFt) has been characterized by UV–Vis spectroscopy, circular dichroism and X-ray diffraction analysis. Data indicate that the protein maintains its fold upon encapsulation of the metallodrug and that Au(I) and Pt(II)-containing fragments are encapsulated within the AFt cage, with Au(I) ion that binds the side chain of Cys126 and Pt(II) in the bulk, respectively. The in vitro cytotoxicity of Pt(II)Au(I)-AFt, as well as that of the free heterobimetallic complex, has been comparatively evaluated on human cervix and breast cancer cells and against cardiomyoblasts and keratinocytes non-tumorigenic cells. Our data demonstrate that it is possible to obtain a protein nanocarrier containing both Pt and Au atoms starting from a bimetallic compound, opening the way for the design and development of new potential drugs based on protein nanocarriers.

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author
; ; ; ; ; ; and
publishing date
type
Contribution to journal
publication status
published
keywords
Protein metalation, Protein nanocage, Protein-metallodrug interactions
in
International Journal of Biological Macromolecules
volume
115
pages
1116 - 1121
publisher
Elsevier
external identifiers
  • scopus:85046628326
  • pmid:29709536
ISSN
0141-8130
DOI
10.1016/j.ijbiomac.2018.04.142
language
English
LU publication?
no
additional info
Publisher Copyright: © 2018 Elsevier B.V.
id
739540ec-4603-4f9d-8e09-c9c782fc8449
date added to LUP
2025-01-21 16:13:41
date last changed
2025-03-04 19:02:29
@article{739540ec-4603-4f9d-8e09-c9c782fc8449,
  abstract     = {{<p>The encapsulation of Pt and Au-based anticancer agents within a protein cage is a promising way to enhance the selectivity of these potential drugs. Here a cytotoxic organometallic compound containing platinum(II) and gold(I) has been encapsulated within a ferritin nanocage (AFt). Inductively plasma coupled mass spectrometry data, collected to evaluate the amount of Pt and Au within the cage, indicate disruption of the starting heterobimetallic complex upon encapsulation within the nanocage. The drug-loaded protein (Pt(II)/Au(I)-AFt) has been characterized by UV–Vis spectroscopy, circular dichroism and X-ray diffraction analysis. Data indicate that the protein maintains its fold upon encapsulation of the metallodrug and that Au(I) and Pt(II)-containing fragments are encapsulated within the AFt cage, with Au(I) ion that binds the side chain of Cys126 and Pt(II) in the bulk, respectively. The in vitro cytotoxicity of Pt(II)Au(I)-AFt, as well as that of the free heterobimetallic complex, has been comparatively evaluated on human cervix and breast cancer cells and against cardiomyoblasts and keratinocytes non-tumorigenic cells. Our data demonstrate that it is possible to obtain a protein nanocarrier containing both Pt and Au atoms starting from a bimetallic compound, opening the way for the design and development of new potential drugs based on protein nanocarriers.</p>}},
  author       = {{Ferraro, Giarita and Petruk, Ganna and Maiore, Laura and Pane, Francesca and Amoresano, Angela and Cinellu, Maria Agostina and Monti, Daria Maria and Merlino, Antonello}},
  issn         = {{0141-8130}},
  keywords     = {{Protein metalation; Protein nanocage; Protein-metallodrug interactions}},
  language     = {{eng}},
  pages        = {{1116--1121}},
  publisher    = {{Elsevier}},
  series       = {{International Journal of Biological Macromolecules}},
  title        = {{Caged noble metals : Encapsulation of a cytotoxic platinum(II)-gold(I) compound within the ferritin nanocage}},
  url          = {{http://dx.doi.org/10.1016/j.ijbiomac.2018.04.142}},
  doi          = {{10.1016/j.ijbiomac.2018.04.142}},
  volume       = {{115}},
  year         = {{2018}},
}