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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...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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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. |
format | Online Article Text |
id | pubmed-9104453 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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