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Fluorinated Protein and Peptide Materials for Biomedical Applications

Fluorination represents one of the most powerful modern design strategies to impart biomacromolecules with unique functionality, empowering them for widespread application in the biomedical realm. However, the properties of fluorinated protein materials remain unpredictable due to the heavy context-...

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Detalles Bibliográficos
Autores principales: Monkovic, Julia M., Gibson, Halle, Sun, Jonathan W., Montclare, Jin Kim
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9609677/
https://www.ncbi.nlm.nih.gov/pubmed/36297312
http://dx.doi.org/10.3390/ph15101201
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author Monkovic, Julia M.
Gibson, Halle
Sun, Jonathan W.
Montclare, Jin Kim
author_facet Monkovic, Julia M.
Gibson, Halle
Sun, Jonathan W.
Montclare, Jin Kim
author_sort Monkovic, Julia M.
collection PubMed
description Fluorination represents one of the most powerful modern design strategies to impart biomacromolecules with unique functionality, empowering them for widespread application in the biomedical realm. However, the properties of fluorinated protein materials remain unpredictable due to the heavy context-dependency of the surrounding atoms influenced by fluorine’s strong electron-withdrawing tendencies. This review aims to discern patterns and elucidate design principles governing the biochemical synthesis and rational installation of fluorine into protein and peptide sequences for diverse biomedical applications. Several case studies are presented to deconvolute the overgeneralized fluorous stabilization effect and critically examine the duplicitous nature of the resultant enhanced chemical and thermostability as it applies to use as biomimetic therapeutics, drug delivery vehicles, and bioimaging modalities.
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spelling pubmed-96096772022-10-28 Fluorinated Protein and Peptide Materials for Biomedical Applications Monkovic, Julia M. Gibson, Halle Sun, Jonathan W. Montclare, Jin Kim Pharmaceuticals (Basel) Review Fluorination represents one of the most powerful modern design strategies to impart biomacromolecules with unique functionality, empowering them for widespread application in the biomedical realm. However, the properties of fluorinated protein materials remain unpredictable due to the heavy context-dependency of the surrounding atoms influenced by fluorine’s strong electron-withdrawing tendencies. This review aims to discern patterns and elucidate design principles governing the biochemical synthesis and rational installation of fluorine into protein and peptide sequences for diverse biomedical applications. Several case studies are presented to deconvolute the overgeneralized fluorous stabilization effect and critically examine the duplicitous nature of the resultant enhanced chemical and thermostability as it applies to use as biomimetic therapeutics, drug delivery vehicles, and bioimaging modalities. MDPI 2022-09-28 /pmc/articles/PMC9609677/ /pubmed/36297312 http://dx.doi.org/10.3390/ph15101201 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 Review
Monkovic, Julia M.
Gibson, Halle
Sun, Jonathan W.
Montclare, Jin Kim
Fluorinated Protein and Peptide Materials for Biomedical Applications
title Fluorinated Protein and Peptide Materials for Biomedical Applications
title_full Fluorinated Protein and Peptide Materials for Biomedical Applications
title_fullStr Fluorinated Protein and Peptide Materials for Biomedical Applications
title_full_unstemmed Fluorinated Protein and Peptide Materials for Biomedical Applications
title_short Fluorinated Protein and Peptide Materials for Biomedical Applications
title_sort fluorinated protein and peptide materials for biomedical applications
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9609677/
https://www.ncbi.nlm.nih.gov/pubmed/36297312
http://dx.doi.org/10.3390/ph15101201
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