The Effect of Cholesterol on Membrane Binding and Self-Assembly of Collagen Fibrils
Collagen is a skeleton of native extracellular matrix (ECM) that is known to provide mechanical and structural stability. In an attempt to develop a new connective cellular model with the surrounding ECM without further experimental complications, such as the reconstitution of ECM receptors, we desi...
Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 36(2020), 26 vom: 07. Juli, Seite 7259-7267 |
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Weitere Verfasser: | , , , |
Format: | Online-Aufsatz |
Sprache: | English |
Veröffentlicht: |
2020
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Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Collagen 9007-34-5 Cholesterol 97C5T2UQ7J |
Zusammenfassung: | Collagen is a skeleton of native extracellular matrix (ECM) that is known to provide mechanical and structural stability. In an attempt to develop a new connective cellular model with the surrounding ECM without further experimental complications, such as the reconstitution of ECM receptors, we designed the experiments and discovered that the fibrillogenesis of membrane-bound collagen is not spontaneous as it is in the form of free collagen in bulk solution. The confocal microscopic results suggest that cholesterol is a crucial component that facilitates the fibril formation on the membrane surface. In situ X-ray and neutron reflectivity on Langmuir monolayer and solid-supported lipid bilayer models, respectively, reveal two features of cholesterol effects on the collagen fibril formation. Mainly, cholesterol increases the lateral lipid headgroup separation on the membrane surface, which promotes the association degree of collagen monomers. It also enhances the elastic modulus of the membrane to impede membrane filtration by the collagen assemblies |
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Beschreibung: | Date Completed 21.06.2021 Date Revised 21.06.2021 published: Print-Electronic Citation Status MEDLINE |
ISSN: | 1520-5827 |
DOI: | 10.1021/acs.langmuir.0c00574 |