Fluorescence study of the interaction between albumin and layered double hydroxides
Este Artículo se encuentra embargado hasta el día 2 de mayo 2025. CiteScore: 7.7 Impact Factor: 4.7 En el siguiente enlace https://www.sciencedirect.com/science/article/abs/pii/S0009279724001200 se encuentra disponible para su lectura: Introduction. Section snippets. Experimental methods. Conclus...
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| Format: | info:eu-repo/semantics/publishedVersion |
| Language: | eng |
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2024
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| Online Access: | http://hdl.handle.net/11086/552450 https://www.sciencedirect.com/science/article/abs/pii/S0009279724001200 https://pubmed.ncbi.nlm.nih.gov/38522563/ https://doi.org/10.1016/j.cbi.2024.110974 |
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| author | Vasti, Cecilia Marengo-Viada, Corina Giacomelli, Carla E. Rojas, Ricardo |
| author2 | https://orcid.org/0009-0006-7267-9659 |
| author_facet | https://orcid.org/0009-0006-7267-9659 Vasti, Cecilia Marengo-Viada, Corina Giacomelli, Carla E. Rojas, Ricardo |
| author_sort | Vasti, Cecilia |
| collection | Repositorio Digital Universitario |
| description | Este Artículo se encuentra embargado hasta el día 2 de mayo 2025.
CiteScore: 7.7
Impact Factor: 4.7
En el siguiente enlace https://www.sciencedirect.com/science/article/abs/pii/S0009279724001200 se encuentra disponible para su lectura: Introduction. Section snippets. Experimental methods. Conclusions. References (43). |
| format | info:eu-repo/semantics/publishedVersion |
| id | rdu-unc.552450 |
| institution | Universidad Nacional de Cordoba |
| language | eng |
| publishDate | 2024 |
| record_format | dspace |
| spelling | rdu-unc.5524502024-06-29T06:23:34Z Fluorescence study of the interaction between albumin and layered double hydroxides Vasti, Cecilia Marengo-Viada, Corina Giacomelli, Carla E. Rojas, Ricardo https://orcid.org/0009-0006-7267-9659 https://orcid.org/0000-0003-4339-3943 https://orcid.org/0000-0001-5826-2036 Surface coverage Quenching Amyloid fibrils Nanoparticles Adsorption Este Artículo se encuentra embargado hasta el día 2 de mayo 2025. CiteScore: 7.7 Impact Factor: 4.7 En el siguiente enlace https://www.sciencedirect.com/science/article/abs/pii/S0009279724001200 se encuentra disponible para su lectura: Introduction. Section snippets. Experimental methods. Conclusions. References (43). info:eu-repo/semantics/publishedVersion Fil: Vasti Cecilia. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Fisicoquímica, Córdoba, Argentina. Fil: Vasti Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Fisicoquímica de Córdoba, Argentina. Fil: Marengo-Viada Corina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Fisicoquímica, Córdoba, Argentina. Fil: Marengo-Viada Corina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Fisicoquímica de Córdoba, Argentina. Fil: Giacomelli Carla E. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Fisicoquímica, Córdoba, Argentina. Fil: Giacomelli Carla E. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Fisicoquímica de Córdoba, Argentina. Fil: Rojas Ricardo. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Fisicoquímica, Córdoba, Argentina. Fil: Rojas Ricardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Fisicoquímica de Córdoba, Argentina. Layered double hydroxides nanoparticles (LDH-NP) are increasingly studied for biomedical applications. Nevertheless, their interaction with biomolecules such as proteins needs further exploration for an effective application. In this work, the adsorption of bovine serum albumin (BSA) on LDH-NP and the conformation changes of the protein upon adsorption were characterized using fluorescence spectroscopy. First, the quenching of tryptophan residues of BSA by chloride-intercalated LDH-NP was explored and the BSA adsorption capacity of LDH-NP were determined. Then, the structural conformation of the protein was analyzed by fluorescence spectroscopy (including synchronous, polarization and quenching studies) at different surface coverages. Finally, the proclivity of adsorbed BSA molecules to assemble as amyloid fibril was evaluated. Due to the positive charging and low curvature of LDH-NP, BSA molecules were strongly adsorbed, which produced a quenching of the protein fluorescence and a large adsorption capacity. The effect on BSA conformation was dependent on surface coverage (SC): at low values, the tryptophan residues were in more hydrophobic environments and more accessible to quenchers than al high ones. At low SC, there is space between the BSA molecules to spread on the surface, which led to a conformation change. Contrarily, the native conformation around tryptophan residues of BSA was preserved at high SC due to the tight packing of the adsorbed protein molecules. As a result, BSA molecules are stabilized against the formation of amyloid fibrils at high SC, while at low SC they present a similar fibrillation than free BSA. info:eu-repo/semantics/publishedVersion Fil: Vasti Cecilia. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Fisicoquímica, Córdoba, Argentina. Fil: Vasti Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Fisicoquímica de Córdoba, Argentina. Fil: Marengo-Viada Corina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Fisicoquímica, Córdoba, Argentina. Fil: Marengo-Viada Corina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Fisicoquímica de Córdoba, Argentina. Fil: Giacomelli Carla E. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Fisicoquímica, Córdoba, Argentina. Fil: Giacomelli Carla E. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Fisicoquímica de Córdoba, Argentina. Fil: Rojas Ricardo. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Fisicoquímica, Córdoba, Argentina. Fil: Rojas Ricardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Fisicoquímica de Córdoba, Argentina. 2024-06-28T22:08:47Z 2024-06-28T22:08:47Z 2024-05-01 article Vasti, C., Marengo-Viada, C., Giacomelli, C. E., & Rojas, R. (2024). Fluorescence study of the interaction between albumin and layered double hydroxides. Chemico-Biological Interactions, 394, 110974 http://hdl.handle.net/11086/552450 0009-2797 https://www.sciencedirect.com/science/article/abs/pii/S0009279724001200 https://pubmed.ncbi.nlm.nih.gov/38522563/ https://doi.org/10.1016/j.cbi.2024.110974 eng Attribution-NonCommercial-NoDerivatives 4.0 International http://creativecommons.org/licenses/by-nc-nd/4.0/ |
| spellingShingle | Surface coverage Quenching Amyloid fibrils Nanoparticles Adsorption Vasti, Cecilia Marengo-Viada, Corina Giacomelli, Carla E. Rojas, Ricardo Fluorescence study of the interaction between albumin and layered double hydroxides |
| title | Fluorescence study of the interaction between albumin and layered double hydroxides |
| title_full | Fluorescence study of the interaction between albumin and layered double hydroxides |
| title_fullStr | Fluorescence study of the interaction between albumin and layered double hydroxides |
| title_full_unstemmed | Fluorescence study of the interaction between albumin and layered double hydroxides |
| title_short | Fluorescence study of the interaction between albumin and layered double hydroxides |
| title_sort | fluorescence study of the interaction between albumin and layered double hydroxides |
| topic | Surface coverage Quenching Amyloid fibrils Nanoparticles Adsorption |
| url | http://hdl.handle.net/11086/552450 https://www.sciencedirect.com/science/article/abs/pii/S0009279724001200 https://pubmed.ncbi.nlm.nih.gov/38522563/ https://doi.org/10.1016/j.cbi.2024.110974 |
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