A new class of polyphenolic carbosilane dendrimers binds human serum albumin in a structure-dependent fashion
Abstract The use of dendrimers as drug and nucleic acid delivery systems requires knowledge of their interactions with objects on their way to the target. In the present work, we investigated the interaction of a new class of carbosilane dendrimers functionalized with polyphenolic and caffeic acid r...
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Nature Portfolio
2024-03-01
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| Series: | Scientific Reports |
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| Online Access: | https://doi.org/10.1038/s41598-024-56509-0 |
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| author | Marika Grodzicka Sylwia Michlewska Adam Buczkowski Szymon Sekowski Cornelia E. Pena-Gonzalez Paula Ortega Francisco Javier de la Mata Janusz Blasiak Maria Bryszewska Maksim Ionov |
| author_facet | Marika Grodzicka Sylwia Michlewska Adam Buczkowski Szymon Sekowski Cornelia E. Pena-Gonzalez Paula Ortega Francisco Javier de la Mata Janusz Blasiak Maria Bryszewska Maksim Ionov |
| author_sort | Marika Grodzicka |
| collection | DOAJ |
| description | Abstract The use of dendrimers as drug and nucleic acid delivery systems requires knowledge of their interactions with objects on their way to the target. In the present work, we investigated the interaction of a new class of carbosilane dendrimers functionalized with polyphenolic and caffeic acid residues with human serum albumin, which is the most abundant blood protein. The addition of dendrimers to albumin solution decreased the zeta potential of albumin/dendrimer complexes as compared to free albumin, increased density of the fibrillary form of albumin, shifted fluorescence spectrum towards longer wavelengths, induced quenching of tryptophan fluorescence, and decreased ellipticity of circular dichroism resulting from a reduction in the albumin α-helix for random coil structural form. Isothermal titration calorimetry showed that, on average, one molecule of albumin was bound by 6–10 molecules of dendrimers. The zeta size confirmed the binding of the dendrimers to albumin. The interaction of dendrimers and albumin depended on the number of caffeic acid residues and polyethylene glycol modifications in the dendrimer structure. In conclusion, carbosilane polyphenolic dendrimers interact with human albumin changing its structure and electrical properties. However, the consequences of such interaction for the efficacy and side effects of these dendrimers as drug/nucleic acid delivery system requires further research. |
| first_indexed | 2024-04-24T23:08:46Z |
| format | Article |
| id | doaj.art-f94d87a0ab784d138a2d3778bd810fe3 |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-04-24T23:08:46Z |
| publishDate | 2024-03-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-f94d87a0ab784d138a2d3778bd810fe32024-03-17T12:23:44ZengNature PortfolioScientific Reports2045-23222024-03-011411910.1038/s41598-024-56509-0A new class of polyphenolic carbosilane dendrimers binds human serum albumin in a structure-dependent fashionMarika Grodzicka0Sylwia Michlewska1Adam Buczkowski2Szymon Sekowski3Cornelia E. Pena-Gonzalez4Paula Ortega5Francisco Javier de la Mata6Janusz Blasiak7Maria Bryszewska8Maksim Ionov9Department of General Biophysics, Faculty of Biology and Environmental Protection, University of LodzLaboratory of Microscopic Imaging and Specialized Biological Techniques, Faculty of Biology and Environmental Protection, University of LodzDivision of Biophysical Chemistry, Department of Physical Chemistry, Faculty of Chemistry, University of LodzLaboratory of Molecular Biophysics, Department of Microbiology and Biotechnology, Faculty of Biology, University of BialystokDepartment of Organic and Inorganic Chemistry, and Research Institute in Chemistry “Andrés M. del Río” (IQAR), Spain and Instituto Ramon y Cajal de Investigacion Sanitaria, IRYCIS, Universidad de AlcaláDepartment of Organic and Inorganic Chemistry, and Research Institute in Chemistry “Andrés M. del Río” (IQAR), Spain and Instituto Ramon y Cajal de Investigacion Sanitaria, IRYCIS, Universidad de AlcaláDepartment of Organic and Inorganic Chemistry, and Research Institute in Chemistry “Andrés M. del Río” (IQAR), Spain and Instituto Ramon y Cajal de Investigacion Sanitaria, IRYCIS, Universidad de AlcaláFaculty of Medicine, Collegium Medicum, Mazovian Academy in PlockDepartment of General Biophysics, Faculty of Biology and Environmental Protection, University of LodzDepartment of General Biophysics, Faculty of Biology and Environmental Protection, University of LodzAbstract The use of dendrimers as drug and nucleic acid delivery systems requires knowledge of their interactions with objects on their way to the target. In the present work, we investigated the interaction of a new class of carbosilane dendrimers functionalized with polyphenolic and caffeic acid residues with human serum albumin, which is the most abundant blood protein. The addition of dendrimers to albumin solution decreased the zeta potential of albumin/dendrimer complexes as compared to free albumin, increased density of the fibrillary form of albumin, shifted fluorescence spectrum towards longer wavelengths, induced quenching of tryptophan fluorescence, and decreased ellipticity of circular dichroism resulting from a reduction in the albumin α-helix for random coil structural form. Isothermal titration calorimetry showed that, on average, one molecule of albumin was bound by 6–10 molecules of dendrimers. The zeta size confirmed the binding of the dendrimers to albumin. The interaction of dendrimers and albumin depended on the number of caffeic acid residues and polyethylene glycol modifications in the dendrimer structure. In conclusion, carbosilane polyphenolic dendrimers interact with human albumin changing its structure and electrical properties. However, the consequences of such interaction for the efficacy and side effects of these dendrimers as drug/nucleic acid delivery system requires further research.https://doi.org/10.1038/s41598-024-56509-0Polyphenolic dendrimersSerum human albuminZeta potentialCircular dichroismIsothermal titration calorimetry |
| spellingShingle | Marika Grodzicka Sylwia Michlewska Adam Buczkowski Szymon Sekowski Cornelia E. Pena-Gonzalez Paula Ortega Francisco Javier de la Mata Janusz Blasiak Maria Bryszewska Maksim Ionov A new class of polyphenolic carbosilane dendrimers binds human serum albumin in a structure-dependent fashion Scientific Reports Polyphenolic dendrimers Serum human albumin Zeta potential Circular dichroism Isothermal titration calorimetry |
| title | A new class of polyphenolic carbosilane dendrimers binds human serum albumin in a structure-dependent fashion |
| title_full | A new class of polyphenolic carbosilane dendrimers binds human serum albumin in a structure-dependent fashion |
| title_fullStr | A new class of polyphenolic carbosilane dendrimers binds human serum albumin in a structure-dependent fashion |
| title_full_unstemmed | A new class of polyphenolic carbosilane dendrimers binds human serum albumin in a structure-dependent fashion |
| title_short | A new class of polyphenolic carbosilane dendrimers binds human serum albumin in a structure-dependent fashion |
| title_sort | new class of polyphenolic carbosilane dendrimers binds human serum albumin in a structure dependent fashion |
| topic | Polyphenolic dendrimers Serum human albumin Zeta potential Circular dichroism Isothermal titration calorimetry |
| url | https://doi.org/10.1038/s41598-024-56509-0 |
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