A correlation between secondary structure and rheological properties of low-density lipoproteins at air/water interfaces

A correlation between secondary structure and rheological properties of low-density lipoproteins... The secondary structure of apolipoprotein B-100 is studied within the bulk phase and at the air/water interface. In these “in viro” experiments, infrared reflection absorption spectroscopy (IRRAS) study was performed at the air/water interface while circular dichroism (CD) was conducted in the bulk phase. In the bulk phase, the conformational structure containing a significant amount of β–structure, whereas varying amount of α-helix, unordered structures, and β-sheet were observed at the air/water interface depending on the low-density lipoprotein (LDL) film interfacial pressure. The present IRRAS results demonstrate the importance of interfacial pressure-induced structural conformations on the apoB-100. A correlation between the secondary structure of the apoB-100 protein and the monomolecular film elasticity at the air/water interface was also established. The orientation of apoB-100 with respect to the LDL film-normal was found to depend on the interfacial pressure exhibited by the monomolecular film. These results may shed light on LDL’s pivotal role in the progression of atherosclerotic coronary artery disease as demonstrated previously by clinical trials. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Biological Physics Springer Journals

A correlation between secondary structure and rheological properties of low-density lipoproteins at air/water interfaces

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Publisher
Springer Netherlands
Copyright
Copyright © 2017 by Springer Science+Business Media B.V.
Subject
Physics; Biological and Medical Physics, Biophysics; Biochemistry, general; Complex Systems; Neurosciences; Soft and Granular Matter, Complex Fluids and Microfluidics
ISSN
0092-0606
eISSN
1573-0689
D.O.I.
10.1007/s10867-017-9458-3
Publisher site
See Article on Publisher Site

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