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231225s2020 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.0c00574
|2 doi
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|a DE-627
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|e rakwb
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|a eng
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|a Phan, Minh D
|e verfasserin
|4 aut
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|a The Effect of Cholesterol on Membrane Binding and Self-Assembly of Collagen Fibrils
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|c 2020
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|a Text
|b txt
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|a ƒaComputermedien
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|a ƒa Online-Ressource
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|a Date Completed 21.06.2021
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|a Date Revised 21.06.2021
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a 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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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Collagen
|2 NLM
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|a 9007-34-5
|2 NLM
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|a Cholesterol
|2 NLM
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|a 97C5T2UQ7J
|2 NLM
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|a Lee, Keel Yong
|e verfasserin
|4 aut
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|a Lee, Jumi
|e verfasserin
|4 aut
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|a Satija, Sushil K
|e verfasserin
|4 aut
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|a Shin, Kwanwoo
|e verfasserin
|4 aut
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 36(2020), 26 vom: 07. Juli, Seite 7259-7267
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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|g volume:36
|g year:2020
|g number:26
|g day:07
|g month:07
|g pages:7259-7267
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|u http://dx.doi.org/10.1021/acs.langmuir.0c00574
|3 Volltext
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