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^*

^*Bu çalışma için yazışmadan sorumlu yazar

City University of New York
University of Minnesota Morris
Boston University

Araştırma sonucu: Dergiye katkı › Makale › bilirkişi

7 Atıf (Scopus)

Özet

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.

Orijinal dil	İngilizce
Sayfa (başlangıç-bitiş)	47-57
Sayfa sayısı	11
Dergi	Biophysical Chemistry
Hacim	218
DOI'lar	https://doi.org/10.1016/j.bpc.2016.09.002
Yayın durumu	Yayınlandı - 1 Kas 2016
Harici olarak yayınlandı	Evet

Bibliyografik not

Publisher Copyright:
© 2016 Elsevier B.V.

Finansman

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.

Finansörler	Finansör numarası
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

Belgeye Erişim

10.1016/j.bpc.2016.09.002

Diğer Dosyalar ve Linkler

Link to publication in Scopus

Alıntı Yap

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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.\}",

note = "Publisher Copyright: {\textcopyright} 2016 Elsevier B.V.",

year = "2016",

month = nov,

day = "1",

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

language = "English",

volume = "218",

pages = "47--57",

journal = "Biophysical Chemistry",

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TY - JOUR

T1 - Mechanical, structural, and dynamical modifications of cholesterol exposed porcine aortic elastin

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

UR - https://www.scopus.com/pages/publications/84988020137

U2 - 10.1016/j.bpc.2016.09.002

DO - 10.1016/j.bpc.2016.09.002

M3 - Article

C2 - 27648754

AN - SCOPUS:84988020137

SN - 0301-4622

VL - 218

SP - 47

EP - 57

JO - Biophysical Chemistry

JF - Biophysical Chemistry

ER -

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

Özet

Bibliyografik not

Finansman

Belgeye Erişim

Diğer Dosyalar ve Linkler

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