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Synchrotron radiation-based Fourier-transform infrared spectromicroscopy for characterization of the protein/peptide distribution in single microspheres
The present study establishes a visualization method for the measurement of the distribution and localization of protein/peptide constituents within a single poly-lactide-co-glycolide (PLGA) microsphere using synchrotron radiation–based Fourier-transform infrared spectromicroscopy (SR-FTIR). The rep...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4629252/ https://www.ncbi.nlm.nih.gov/pubmed/26579456 http://dx.doi.org/10.1016/j.apsb.2015.03.008 |
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author | Wang, Manli Lu, Xiaolong Yin, Xianzhen Tong, Yajun Peng, Weiwei Wu, Li Li, Haiyan Yang, Yan Gu, Jingkai Xiao, Tiqiao Chen, Min Zhang, Jiwen |
author_facet | Wang, Manli Lu, Xiaolong Yin, Xianzhen Tong, Yajun Peng, Weiwei Wu, Li Li, Haiyan Yang, Yan Gu, Jingkai Xiao, Tiqiao Chen, Min Zhang, Jiwen |
author_sort | Wang, Manli |
collection | PubMed |
description | The present study establishes a visualization method for the measurement of the distribution and localization of protein/peptide constituents within a single poly-lactide-co-glycolide (PLGA) microsphere using synchrotron radiation–based Fourier-transform infrared spectromicroscopy (SR-FTIR). The representative infrared wavenumbers specific for protein/peptide (Exenatide) and excipient (PLGA) were identified and chemical maps at the single microsphere level were generated by measuring and plotting the intensity of these specific bands. For quantitative analysis of the distribution within microspheres, Matlab software was used to transform the map file into a 3D matrix and the matrix values specific for the drug and excipient were extracted. Comparison of the normalized SR-FTIR maps of PLGA and Exenatide indicated that PLGA was uniformly distributed, while Exenatide was relatively non-uniformly distributed in the microspheres. In conclusion, SR-FTIR is a rapid, nondestructive and sensitive detection technology to provide the distribution of chemical constituents and functional groups in microparticles and microspheres. |
format | Online Article Text |
id | pubmed-4629252 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-46292522015-11-17 Synchrotron radiation-based Fourier-transform infrared spectromicroscopy for characterization of the protein/peptide distribution in single microspheres Wang, Manli Lu, Xiaolong Yin, Xianzhen Tong, Yajun Peng, Weiwei Wu, Li Li, Haiyan Yang, Yan Gu, Jingkai Xiao, Tiqiao Chen, Min Zhang, Jiwen Acta Pharm Sin B Original Article The present study establishes a visualization method for the measurement of the distribution and localization of protein/peptide constituents within a single poly-lactide-co-glycolide (PLGA) microsphere using synchrotron radiation–based Fourier-transform infrared spectromicroscopy (SR-FTIR). The representative infrared wavenumbers specific for protein/peptide (Exenatide) and excipient (PLGA) were identified and chemical maps at the single microsphere level were generated by measuring and plotting the intensity of these specific bands. For quantitative analysis of the distribution within microspheres, Matlab software was used to transform the map file into a 3D matrix and the matrix values specific for the drug and excipient were extracted. Comparison of the normalized SR-FTIR maps of PLGA and Exenatide indicated that PLGA was uniformly distributed, while Exenatide was relatively non-uniformly distributed in the microspheres. In conclusion, SR-FTIR is a rapid, nondestructive and sensitive detection technology to provide the distribution of chemical constituents and functional groups in microparticles and microspheres. Elsevier 2015-05 2015-04-14 /pmc/articles/PMC4629252/ /pubmed/26579456 http://dx.doi.org/10.1016/j.apsb.2015.03.008 Text en © 2015 Chinese Pharmaceutical Association and Institute of Materia Medica, Chinese Academy of Medical Sciences. Production and hosting by Elsevier B.V. http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Original Article Wang, Manli Lu, Xiaolong Yin, Xianzhen Tong, Yajun Peng, Weiwei Wu, Li Li, Haiyan Yang, Yan Gu, Jingkai Xiao, Tiqiao Chen, Min Zhang, Jiwen Synchrotron radiation-based Fourier-transform infrared spectromicroscopy for characterization of the protein/peptide distribution in single microspheres |
title | Synchrotron radiation-based Fourier-transform infrared spectromicroscopy for characterization of the protein/peptide distribution in single microspheres |
title_full | Synchrotron radiation-based Fourier-transform infrared spectromicroscopy for characterization of the protein/peptide distribution in single microspheres |
title_fullStr | Synchrotron radiation-based Fourier-transform infrared spectromicroscopy for characterization of the protein/peptide distribution in single microspheres |
title_full_unstemmed | Synchrotron radiation-based Fourier-transform infrared spectromicroscopy for characterization of the protein/peptide distribution in single microspheres |
title_short | Synchrotron radiation-based Fourier-transform infrared spectromicroscopy for characterization of the protein/peptide distribution in single microspheres |
title_sort | synchrotron radiation-based fourier-transform infrared spectromicroscopy for characterization of the protein/peptide distribution in single microspheres |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4629252/ https://www.ncbi.nlm.nih.gov/pubmed/26579456 http://dx.doi.org/10.1016/j.apsb.2015.03.008 |
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