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Title: The Effect of Cholesterol on Membrane Binding and Self-Assembly of Collagen Fibrils

Journal Article · · Langmuir
ORCiD logo [1];  [2];  [3];  [4]; ORCiD logo [3]
  1. Sogang Univ., Seoul (South Korea). Inst. of Biological Interfaces; Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
  2. Sogang Univ., Seoul (South Korea). Inst. of Biological Interfaces; Harvard Univ., Cambridge, MA (United States)
  3. Sogang Univ., Seoul (South Korea). Inst. of Biological Interfaces
  4. National Inst. of Standards and Technology (NIST), Gaithersburg, MD (United States). Center for Neutron Research

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. Furthermore, 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.

Research Organization:
Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)
Sponsoring Organization:
USDOE
Grant/Contract Number:
AC05-00OR22725
OSTI ID:
1785169
Journal Information:
Langmuir, Vol. 36, Issue 26; ISSN 0743-7463
Publisher:
American Chemical SocietyCopyright Statement
Country of Publication:
United States
Language:
English

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