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

doi:10.1016/j.bpc.2016.09.002

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^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

6 Citations (Scopus)

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 language	English
Pages (from-to)	47-57
Number of pages	11
Journal	Biophysical Chemistry
Volume	218
DOIs	https://doi.org/10.1016/j.bpc.2016.09.002
Publication status	Published - 1 Nov 2016
Externally published	Yes

Bibliographical note

Publisher Copyright:
© 2016 Elsevier B.V.

Funding

G.S.B. acknowledges support from the National Institutes of Health under award number 2SC1GM086268 . Y. Z. acknowledges support from Kenneth R. Lutchen Distinguished Fellowship from the College of Engineering, Student Research Award from the Undergraduate Research Opportunities Program (UROP) at Boston University, National Science Foundation grants CMMI 1100791 (Research Experiences for Undergraduates) and CMMI 1463390 . Collection of data at the New York Structural Biology Center was made possible by a grant from NYSTAR.This research was supported, in part, under National Science Foundation Grants CNS-0958379, CNS-0855217, ACI-1126113 and the City University of New York High Performance ComputingCenter at the College of Staten Island.

Funders	Funder number
City University of New York High Performance ComputingCenter at the College of Staten Island
National Science Foundation	CNS-0958379, ACI-1126113, CNS-0855217, CMMI 1463390, CMMI 1100791
National Institutes of Health
National Institute of General Medical Sciences	SC1GM086268
Boston University

Keywords

C MAS NMR
Cholesterol
Elastin
H NMR

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10.1016/j.bpc.2016.09.002

Cite this

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

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.",

keywords = "C MAS NMR, Cholesterol, Elastin, H NMR",

author = "Kubra Bilici and Morgan, {Steven W.} and Silverstein, {Moshe C.} and Yunjie Wang and Sun, {Hyung Jin} and Yanhang Zhang and Boutis, {Gregory S.}",

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doi = "10.1016/j.bpc.2016.09.002",

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AU - Bilici, Kubra

AU - Morgan, Steven W.

AU - Silverstein, Moshe C.

AU - Wang, Yunjie

AU - Sun, Hyung Jin

AU - Zhang, Yanhang

AU - Boutis, Gregory S.

PY - 2016/11/1

Y1 - 2016/11/1

N2 - 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.

AB - 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.

KW - C MAS NMR

KW - Cholesterol

KW - Elastin

KW - H NMR

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SN - 0301-4622

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JO - Biophysical Chemistry

JF - Biophysical Chemistry

ER -

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

Abstract

Bibliographical note

Funding

Keywords

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