Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Canziani, Letizia, Marenco, Manuela, Cavenaghi, Giorgio, Manfrinato, Giulia, Taglietti, Angelo, Girella, Alessandro, Aprile, Carlo, Pepe, Giovanna, Lodola, Lorenzo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
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
_version_ 1784637180734341120
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
work_keys_str_mv AT canzianiletizia chemicalandphysicalcharacterisationofmacroaggregatedhumanserumalbuminstrengthandspecificityofbondswith99mtcand68ga
AT marencomanuela chemicalandphysicalcharacterisationofmacroaggregatedhumanserumalbuminstrengthandspecificityofbondswith99mtcand68ga
AT cavenaghigiorgio chemicalandphysicalcharacterisationofmacroaggregatedhumanserumalbuminstrengthandspecificityofbondswith99mtcand68ga
AT manfrinatogiulia chemicalandphysicalcharacterisationofmacroaggregatedhumanserumalbuminstrengthandspecificityofbondswith99mtcand68ga
AT tagliettiangelo chemicalandphysicalcharacterisationofmacroaggregatedhumanserumalbuminstrengthandspecificityofbondswith99mtcand68ga
AT girellaalessandro chemicalandphysicalcharacterisationofmacroaggregatedhumanserumalbuminstrengthandspecificityofbondswith99mtcand68ga
AT aprilecarlo chemicalandphysicalcharacterisationofmacroaggregatedhumanserumalbuminstrengthandspecificityofbondswith99mtcand68ga
AT pepegiovanna chemicalandphysicalcharacterisationofmacroaggregatedhumanserumalbuminstrengthandspecificityofbondswith99mtcand68ga
AT lodolalorenzo chemicalandphysicalcharacterisationofmacroaggregatedhumanserumalbuminstrengthandspecificityofbondswith99mtcand68ga