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(Macro)Molecular Imprinting of Proteins on PCL Electrospun Scaffolds
[Image: see text] Biological recognition sites are very useful for biomedical purposes and, more specifically, for polymeric scaffolds. However, synthetic polymers are not capable of providing specific biological recognition sites. To solve this inconvenience, functionalization of biological moietie...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American
Chemical Society
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8289240/ https://www.ncbi.nlm.nih.gov/pubmed/34128651 http://dx.doi.org/10.1021/acsami.1c04022 |
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author | Perez-Puyana, Victor Wieringa, Paul Guerrero, Antonio Romero, Alberto Moroni, Lorenzo |
author_facet | Perez-Puyana, Victor Wieringa, Paul Guerrero, Antonio Romero, Alberto Moroni, Lorenzo |
author_sort | Perez-Puyana, Victor |
collection | PubMed |
description | [Image: see text] Biological recognition sites are very useful for biomedical purposes and, more specifically, for polymeric scaffolds. However, synthetic polymers are not capable of providing specific biological recognition sites. To solve this inconvenience, functionalization of biological moieties is typically performed, oftentimes via peptide binding. In this sense, the main task is capturing the biological complexity of a protein. This study proposes a possible alternative solution to this challenge. Our approach is based on the combination of molecular imprinting (MI) and electrospinning processes. We propose here an alternative MI approach with polymeric structures, instead of using cross-linkers and monomers as conventionally performed. Different PCL–protein scaffolds were produced via electrospinning before performing MI. Gelatin, collagen, and elastin were used as proteins. Results evidenced that the MI process conducted with PCL electrospun membranes was carried out with ionic interactions between the desired molecules and the recognition sites formed. In addition, it has been proved that MI was more efficient when using gelatin as a template. This approach opens a new stage in the development of recognition sites in scaffolds obtained with synthetic polymers and their application for biomedical purposes. |
format | Online Article Text |
id | pubmed-8289240 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American
Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-82892402021-07-20 (Macro)Molecular Imprinting of Proteins on PCL Electrospun Scaffolds Perez-Puyana, Victor Wieringa, Paul Guerrero, Antonio Romero, Alberto Moroni, Lorenzo ACS Appl Mater Interfaces [Image: see text] Biological recognition sites are very useful for biomedical purposes and, more specifically, for polymeric scaffolds. However, synthetic polymers are not capable of providing specific biological recognition sites. To solve this inconvenience, functionalization of biological moieties is typically performed, oftentimes via peptide binding. In this sense, the main task is capturing the biological complexity of a protein. This study proposes a possible alternative solution to this challenge. Our approach is based on the combination of molecular imprinting (MI) and electrospinning processes. We propose here an alternative MI approach with polymeric structures, instead of using cross-linkers and monomers as conventionally performed. Different PCL–protein scaffolds were produced via electrospinning before performing MI. Gelatin, collagen, and elastin were used as proteins. Results evidenced that the MI process conducted with PCL electrospun membranes was carried out with ionic interactions between the desired molecules and the recognition sites formed. In addition, it has been proved that MI was more efficient when using gelatin as a template. This approach opens a new stage in the development of recognition sites in scaffolds obtained with synthetic polymers and their application for biomedical purposes. American Chemical Society 2021-06-15 2021-06-30 /pmc/articles/PMC8289240/ /pubmed/34128651 http://dx.doi.org/10.1021/acsami.1c04022 Text en © 2021 The Authors. Published by American Chemical Society Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Perez-Puyana, Victor Wieringa, Paul Guerrero, Antonio Romero, Alberto Moroni, Lorenzo (Macro)Molecular Imprinting of Proteins on PCL Electrospun Scaffolds |
title | (Macro)Molecular
Imprinting of Proteins on PCL Electrospun
Scaffolds |
title_full | (Macro)Molecular
Imprinting of Proteins on PCL Electrospun
Scaffolds |
title_fullStr | (Macro)Molecular
Imprinting of Proteins on PCL Electrospun
Scaffolds |
title_full_unstemmed | (Macro)Molecular
Imprinting of Proteins on PCL Electrospun
Scaffolds |
title_short | (Macro)Molecular
Imprinting of Proteins on PCL Electrospun
Scaffolds |
title_sort | (macro)molecular
imprinting of proteins on pcl electrospun
scaffolds |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8289240/ https://www.ncbi.nlm.nih.gov/pubmed/34128651 http://dx.doi.org/10.1021/acsami.1c04022 |
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