Mechanical, structural, and dynamical modifications of cholesterol exposed porcine aortic elastin

Kubra Bilici, Steven W. Morgan, Moshe C. Silverstein, Yunjie Wang, Hyung Jin Sun, Yanhang Zhang, Gregory S. Boutis

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

Elastin is a protein of the extracellular matrix that contributes significantly to the elasticity of connective tissues. In this study, we examine dynamical and structural modifications of aortic elastin exposed to cholesterol by NMR spectroscopic and relaxation methodologies. Macroscopic measurements are also presented and reveal that cholesterol treatment may cause a decrease in the stiffness of tissue. 2H NMR relaxation techniques revealed differences between the relative populations of water that correlate with the swelling of the tissue following cholesterol exposure. 13C magic-angle-spinning NMR spectroscopy and relaxation methods indicate that cholesterol treated aortic elastin is more mobile than control samples. Molecular dynamics simulations on a short elastin repeat VPGVG in the presence of cholesterol are used to investigate the energetic and entropic contributions to the retractive force, in comparison to the same peptide in water. Peptide stiffness is observed to reduce following cholesterol exposure due to a decrease in the entropic force.

Original languageEnglish (US)
Pages (from-to)47-57
Number of pages11
JournalBiophysical Chemistry
Volume218
DOIs
StatePublished - Nov 1 2016

Bibliographical note

Publisher Copyright:
© 2016 Elsevier B.V.

Keywords

  • C MAS NMR
  • Cholesterol
  • Elastin
  • H NMR

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