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Cubic and Hexagonal Mesophases for Protein Encapsulation: Structural Effects of Insulin Confinement
[Image: see text] Monoolein-based cubic and hexagonal mesophases were investigated as matrices for insulin loading, at low pH, as a function of temperature and in the presence of increasing amounts of oleic acid, as a structural stabilizer for the hexagonal phase. Synchrotron small angle X-ray diffr...
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/PMC8397388/ https://www.ncbi.nlm.nih.gov/pubmed/34369787 http://dx.doi.org/10.1021/acs.langmuir.1c01587 |
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author | Astolfi, Paola Giorgini, Elisabetta Perinelli, Diego Romano Vita, Francesco Adamo, Fabrizio Corrado Logrippo, Serena Parlapiano, Marco Bonacucina, Giulia Pucciarelli, Stefania Francescangeli, Oriano Vaccari, Lisa Pisani, Michela |
author_facet | Astolfi, Paola Giorgini, Elisabetta Perinelli, Diego Romano Vita, Francesco Adamo, Fabrizio Corrado Logrippo, Serena Parlapiano, Marco Bonacucina, Giulia Pucciarelli, Stefania Francescangeli, Oriano Vaccari, Lisa Pisani, Michela |
author_sort | Astolfi, Paola |
collection | PubMed |
description | [Image: see text] Monoolein-based cubic and hexagonal mesophases were investigated as matrices for insulin loading, at low pH, as a function of temperature and in the presence of increasing amounts of oleic acid, as a structural stabilizer for the hexagonal phase. Synchrotron small angle X-ray diffraction, rheological measurements, and attenuated total reflection-Fourier transform infrared spectroscopy were used to study the effects of insulin loading on the lipid mesophases and of the effect of protein confinement in the 2D- and 3D-lipid matrix water channels on its stability and unfolding behavior. We found that insulin encapsulation has only little effects both on the mesophase structures and on the viscoelastic properties of lipid systems, whereas protein confinement affects the response of the secondary structure of insulin to thermal changes in a different manner according to the specific mesophase: in the cubic structure, the unfolding toward an unordered structure is favored, while the prevalence of parallel β-sheets, and nuclei for fibril formation, is observed in hexagonal structures. |
format | Online Article Text |
id | pubmed-8397388 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-83973882021-08-31 Cubic and Hexagonal Mesophases for Protein Encapsulation: Structural Effects of Insulin Confinement Astolfi, Paola Giorgini, Elisabetta Perinelli, Diego Romano Vita, Francesco Adamo, Fabrizio Corrado Logrippo, Serena Parlapiano, Marco Bonacucina, Giulia Pucciarelli, Stefania Francescangeli, Oriano Vaccari, Lisa Pisani, Michela Langmuir [Image: see text] Monoolein-based cubic and hexagonal mesophases were investigated as matrices for insulin loading, at low pH, as a function of temperature and in the presence of increasing amounts of oleic acid, as a structural stabilizer for the hexagonal phase. Synchrotron small angle X-ray diffraction, rheological measurements, and attenuated total reflection-Fourier transform infrared spectroscopy were used to study the effects of insulin loading on the lipid mesophases and of the effect of protein confinement in the 2D- and 3D-lipid matrix water channels on its stability and unfolding behavior. We found that insulin encapsulation has only little effects both on the mesophase structures and on the viscoelastic properties of lipid systems, whereas protein confinement affects the response of the secondary structure of insulin to thermal changes in a different manner according to the specific mesophase: in the cubic structure, the unfolding toward an unordered structure is favored, while the prevalence of parallel β-sheets, and nuclei for fibril formation, is observed in hexagonal structures. American Chemical Society 2021-08-09 2021-08-24 /pmc/articles/PMC8397388/ /pubmed/34369787 http://dx.doi.org/10.1021/acs.langmuir.1c01587 Text en © 2021 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by/4.0/Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Astolfi, Paola Giorgini, Elisabetta Perinelli, Diego Romano Vita, Francesco Adamo, Fabrizio Corrado Logrippo, Serena Parlapiano, Marco Bonacucina, Giulia Pucciarelli, Stefania Francescangeli, Oriano Vaccari, Lisa Pisani, Michela Cubic and Hexagonal Mesophases for Protein Encapsulation: Structural Effects of Insulin Confinement |
title | Cubic and Hexagonal Mesophases for Protein Encapsulation:
Structural Effects of Insulin Confinement |
title_full | Cubic and Hexagonal Mesophases for Protein Encapsulation:
Structural Effects of Insulin Confinement |
title_fullStr | Cubic and Hexagonal Mesophases for Protein Encapsulation:
Structural Effects of Insulin Confinement |
title_full_unstemmed | Cubic and Hexagonal Mesophases for Protein Encapsulation:
Structural Effects of Insulin Confinement |
title_short | Cubic and Hexagonal Mesophases for Protein Encapsulation:
Structural Effects of Insulin Confinement |
title_sort | cubic and hexagonal mesophases for protein encapsulation:
structural effects of insulin confinement |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8397388/ https://www.ncbi.nlm.nih.gov/pubmed/34369787 http://dx.doi.org/10.1021/acs.langmuir.1c01587 |
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