Cubic and Hexagonal Mesophases for Protein Encapsulation : Structural Effects of Insulin Confinement

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, rheologica...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 37(2021), 33 vom: 24. Aug., Seite 10166-10176
1. Verfasser: Astolfi, Paola (VerfasserIn)
Weitere Verfasser: Giorgini, Elisabetta, Perinelli, Diego Romano, Vita, Francesco, Adamo, Fabrizio Corrado, Logrippo, Serena, Parlapiano, Marco, Bonacucina, Giulia, Pucciarelli, Stefania, Francescangeli, Oriano, Vaccari, Lisa, Pisani, Michela
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2021
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Insulin
Beschreibung
Zusammenfassung: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
Beschreibung:Date Completed 26.08.2021
Date Revised 01.09.2021
published: Print-Electronic
Citation Status MEDLINE
ISSN:1520-5827
DOI:10.1021/acs.langmuir.1c01587