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Albumin Binds Doxorubicin via Self–Assembling Dyes as Specific Polymolecular Ligands

Congo red (CR) type self–assembled ribbon–like structures (SRLS) were previously shown to interact with some proteins, including albumin. SRLS also complex with some drugs with a flat, ring–shaped structure with aromatic characteristics, intercalating them into their ribbon structure. The combinatio...

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Autores principales: Jagusiak, Anna, Chłopaś, Katarzyna, Zemanek, Grzegorz, Kościk, Izabela, Skorek, Paweł, Stopa, Barbara
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9104453/
https://www.ncbi.nlm.nih.gov/pubmed/35563426
http://dx.doi.org/10.3390/ijms23095033
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author Jagusiak, Anna
Chłopaś, Katarzyna
Zemanek, Grzegorz
Kościk, Izabela
Skorek, Paweł
Stopa, Barbara
author_facet Jagusiak, Anna
Chłopaś, Katarzyna
Zemanek, Grzegorz
Kościk, Izabela
Skorek, Paweł
Stopa, Barbara
author_sort Jagusiak, Anna
collection PubMed
description Congo red (CR) type self–assembled ribbon–like structures (SRLS) were previously shown to interact with some proteins, including albumin. SRLS also complex with some drugs with a flat, ring–shaped structure with aromatic characteristics, intercalating them into their ribbon structure. The combination of interaction with proteins and drug binding by SRLS enables the use of such systems for immunotargeting. It is especially interesting in the case of chemotherapeutic agents. The present experiments aimed to show that the model carrier system composed of supramolecular albumin and Congo red efficiently binds doxorubicin (Dox) and that the drug can be released at reduced pH. The presented results come from the studies on such complexes differing in the molar ratio of CR to Dox. The following methods were used for the analysis: electrophoresis, dialysis, gel filtration, spectral analysis, and analysis of the size of the hydrodynamic radius using the dynamic light scattering method (DLS). The applied methods confirmed the formation of the CR–Dox complex, with large dimensions and changed properties compared with free CR. The presented results show that albumin binds both CR and its complex with Dox. Various CR–Dox molar ratios, 5:1, 2:1, and 1:1, were analyzed. The confirmation of the possibility of releasing the drug from the carriers thus formed was also obtained. The presented research is important due to the search for optimal solutions for the use of SRLS in drug immunotargeting, with particular emphasis on chemotherapeutic agents.
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spelling pubmed-91044532022-05-14 Albumin Binds Doxorubicin via Self–Assembling Dyes as Specific Polymolecular Ligands Jagusiak, Anna Chłopaś, Katarzyna Zemanek, Grzegorz Kościk, Izabela Skorek, Paweł Stopa, Barbara Int J Mol Sci Article Congo red (CR) type self–assembled ribbon–like structures (SRLS) were previously shown to interact with some proteins, including albumin. SRLS also complex with some drugs with a flat, ring–shaped structure with aromatic characteristics, intercalating them into their ribbon structure. The combination of interaction with proteins and drug binding by SRLS enables the use of such systems for immunotargeting. It is especially interesting in the case of chemotherapeutic agents. The present experiments aimed to show that the model carrier system composed of supramolecular albumin and Congo red efficiently binds doxorubicin (Dox) and that the drug can be released at reduced pH. The presented results come from the studies on such complexes differing in the molar ratio of CR to Dox. The following methods were used for the analysis: electrophoresis, dialysis, gel filtration, spectral analysis, and analysis of the size of the hydrodynamic radius using the dynamic light scattering method (DLS). The applied methods confirmed the formation of the CR–Dox complex, with large dimensions and changed properties compared with free CR. The presented results show that albumin binds both CR and its complex with Dox. Various CR–Dox molar ratios, 5:1, 2:1, and 1:1, were analyzed. The confirmation of the possibility of releasing the drug from the carriers thus formed was also obtained. The presented research is important due to the search for optimal solutions for the use of SRLS in drug immunotargeting, with particular emphasis on chemotherapeutic agents. MDPI 2022-05-01 /pmc/articles/PMC9104453/ /pubmed/35563426 http://dx.doi.org/10.3390/ijms23095033 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/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 (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Jagusiak, Anna
Chłopaś, Katarzyna
Zemanek, Grzegorz
Kościk, Izabela
Skorek, Paweł
Stopa, Barbara
Albumin Binds Doxorubicin via Self–Assembling Dyes as Specific Polymolecular Ligands
title Albumin Binds Doxorubicin via Self–Assembling Dyes as Specific Polymolecular Ligands
title_full Albumin Binds Doxorubicin via Self–Assembling Dyes as Specific Polymolecular Ligands
title_fullStr Albumin Binds Doxorubicin via Self–Assembling Dyes as Specific Polymolecular Ligands
title_full_unstemmed Albumin Binds Doxorubicin via Self–Assembling Dyes as Specific Polymolecular Ligands
title_short Albumin Binds Doxorubicin via Self–Assembling Dyes as Specific Polymolecular Ligands
title_sort albumin binds doxorubicin via self–assembling dyes as specific polymolecular ligands
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9104453/
https://www.ncbi.nlm.nih.gov/pubmed/35563426
http://dx.doi.org/10.3390/ijms23095033
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