4.6 Article

Surface properties of collagen-functionalized aluminosilicate particles embedding iron and dysprosium designed for cancer therapy

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JOURNAL OF MOLECULAR STRUCTURE
卷 1236, 期 -, 页码 -

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ELSEVIER
DOI: 10.1016/j.molstruc.2021.130341

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Aluminosilicate particles; Iron; Dysprosium; Collagen; FTIR; XPS

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The study focused on sol-gel derived particles functionalized with type I collagen, with the addition of Fe2O3 for hyperthermia and Dy2O3 for internal radiation therapy. The results showed protein anchoring on the particle surface in a few nanometers thin layer, with some relative changes in protein secondary structure. The secondary structure of collagen mainly consisted of α-helices after interface processes with the particle surface.
Simultaneous radiotherapy and hyperthermia yield synergistic improvement of therapeutic efficacy in cancer therapy. The study is focussed on sol-gel derived particles of 60SiO(2)center dot 20Al(2)O(3)center dot 10Fe(2)O(3)center dot 10Dy(2)O(3) (mol%) system functionalized with type I collagen. The addition to aluminosilicate matrix of Fe2O3 center dot was thought for hyperthermia and of Dy2O3 for internal radiation therapy after neutron activation of dysprosium to Dy-165 radioisotope. The collagen functionalization of these particles aimed to make them well accepted in the body and to contribute to destruction of reactive oxygen species, what has to be taken into account when nanoparticles are used for cancer therapy. The XRD, FTIR and XPS investigations were carried out on Fe-Dy-aluminosilicate particles of average size around tens of nanometers, before and after their incubation in collagen solution in order to prove the protein functionalization particles and to assess the changes in secondary structure of protein following this process. The results show the anchoring of the protein on particles surface in a few nanometers thin layer as well as some relative changes of protein secondary structure. After interface processes with particles surface, the secondary structure of amide I in collagen consists overwhelmingly of a-helices and only about 12 % of beta-turns structure. (C) 2021 Elsevier B.V. All rights reserved.

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