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Chemical and Physical Characterisation of Macroaggregated Human Serum Albumin: Strength and Specificity of Bonds with (99m)Tc and (68)Ga
Background: Macroaggregated human serum albumin (MAA) properties are widely used in nuclear medicine, labelled with (99m)Tc. The aim of this study is to improve the knowledge about the morphology, size, dimension and physical–chemical characteristics of MAA and their bond with (99m)Tc and (68)Ga. Me...
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/PMC8777888/ https://www.ncbi.nlm.nih.gov/pubmed/35056719 http://dx.doi.org/10.3390/molecules27020404 |
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author | Canziani, Letizia Marenco, Manuela Cavenaghi, Giorgio Manfrinato, Giulia Taglietti, Angelo Girella, Alessandro Aprile, Carlo Pepe, Giovanna Lodola, Lorenzo |
author_facet | Canziani, Letizia Marenco, Manuela Cavenaghi, Giorgio Manfrinato, Giulia Taglietti, Angelo Girella, Alessandro Aprile, Carlo Pepe, Giovanna Lodola, Lorenzo |
author_sort | Canziani, Letizia |
collection | PubMed |
description | Background: Macroaggregated human serum albumin (MAA) properties are widely used in nuclear medicine, labelled with (99m)Tc. The aim of this study is to improve the knowledge about the morphology, size, dimension and physical–chemical characteristics of MAA and their bond with (99m)Tc and (68)Ga. Methods: Commercial kits of MAA (Pulmocis(®)) were used. Characterisation through experiments based on SEM, DLS and Stokes’ Law were carried out. In vitro experiments for Langmuir isotherms and pH studies on radiolabelling were performed and the stability of the radiometal complex was verified through competition reactions. Results: The study settles the MAA dimension within the range 43–51 μm. The Langmuir isotherm reveals for [(99m)Tc]MAA: Bmax (46.32), h (2.36); for [(68)Ga]MAA: Bmax (44.54), h (0.893). Dual labelling reveals that MAA does not discriminate different radioisotopes. Experiments on pH placed the optimal pH for labelling with (99m)Tc at 6. Conclusion: Radiolabelling of MAA is possible with high efficiency. The nondiscriminatory MAA bonds make this drug suitable for radiolabelling with different radioisotopes or for dual labelling. This finding illustrates the need to continue investigating MAA chemical and physical characteristics to allow for secure labelling with different isotopes. |
format | Online Article Text |
id | pubmed-8777888 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-87778882022-01-22 Chemical and Physical Characterisation of Macroaggregated Human Serum Albumin: Strength and Specificity of Bonds with (99m)Tc and (68)Ga Canziani, Letizia Marenco, Manuela Cavenaghi, Giorgio Manfrinato, Giulia Taglietti, Angelo Girella, Alessandro Aprile, Carlo Pepe, Giovanna Lodola, Lorenzo Molecules Article Background: Macroaggregated human serum albumin (MAA) properties are widely used in nuclear medicine, labelled with (99m)Tc. The aim of this study is to improve the knowledge about the morphology, size, dimension and physical–chemical characteristics of MAA and their bond with (99m)Tc and (68)Ga. Methods: Commercial kits of MAA (Pulmocis(®)) were used. Characterisation through experiments based on SEM, DLS and Stokes’ Law were carried out. In vitro experiments for Langmuir isotherms and pH studies on radiolabelling were performed and the stability of the radiometal complex was verified through competition reactions. Results: The study settles the MAA dimension within the range 43–51 μm. The Langmuir isotherm reveals for [(99m)Tc]MAA: Bmax (46.32), h (2.36); for [(68)Ga]MAA: Bmax (44.54), h (0.893). Dual labelling reveals that MAA does not discriminate different radioisotopes. Experiments on pH placed the optimal pH for labelling with (99m)Tc at 6. Conclusion: Radiolabelling of MAA is possible with high efficiency. The nondiscriminatory MAA bonds make this drug suitable for radiolabelling with different radioisotopes or for dual labelling. This finding illustrates the need to continue investigating MAA chemical and physical characteristics to allow for secure labelling with different isotopes. MDPI 2022-01-09 /pmc/articles/PMC8777888/ /pubmed/35056719 http://dx.doi.org/10.3390/molecules27020404 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 Canziani, Letizia Marenco, Manuela Cavenaghi, Giorgio Manfrinato, Giulia Taglietti, Angelo Girella, Alessandro Aprile, Carlo Pepe, Giovanna Lodola, Lorenzo Chemical and Physical Characterisation of Macroaggregated Human Serum Albumin: Strength and Specificity of Bonds with (99m)Tc and (68)Ga |
title | Chemical and Physical Characterisation of Macroaggregated Human Serum Albumin: Strength and Specificity of Bonds with (99m)Tc and (68)Ga |
title_full | Chemical and Physical Characterisation of Macroaggregated Human Serum Albumin: Strength and Specificity of Bonds with (99m)Tc and (68)Ga |
title_fullStr | Chemical and Physical Characterisation of Macroaggregated Human Serum Albumin: Strength and Specificity of Bonds with (99m)Tc and (68)Ga |
title_full_unstemmed | Chemical and Physical Characterisation of Macroaggregated Human Serum Albumin: Strength and Specificity of Bonds with (99m)Tc and (68)Ga |
title_short | Chemical and Physical Characterisation of Macroaggregated Human Serum Albumin: Strength and Specificity of Bonds with (99m)Tc and (68)Ga |
title_sort | chemical and physical characterisation of macroaggregated human serum albumin: strength and specificity of bonds with (99m)tc and (68)ga |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8777888/ https://www.ncbi.nlm.nih.gov/pubmed/35056719 http://dx.doi.org/10.3390/molecules27020404 |
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