Shape of tropoelastin, the highly extensible protein that controls human tissue elasticity

Clair Baldock, Andres Oberhauser, Liang Ma, Donna Lammie, Veronique Siegler, Suzanne M. Mithieux, Yidong Tu, John Yuen Ho Chow, Farhana Suleman, Marc Malfois, Sarah Rogers, Liang Guo, Thomas C. Irving, Tim J. Wess, Anthony S. Weiss

Research output: Contribution to journalArticle

104 Citations (Scopus)

Abstract

Elastin enables the reversible deformation of elastic tissues and can withstand decades of repetitive forces. Tropoelastin is the soluble precursor to elastin, the main elastic protein found in mammals. Little is known of the shape and mechanism of assembly of tropoelastin as its unique composition and propensity to self-associate has hampered structural studies. In this study, we solve the nanostructure of full-length and corresponding overlapping fragments of tropoelastin using small angle X-ray and neutron scattering, allowing us to identify discrete regions of the molecule. Tropoelastin is an asymmetric coil, with a protruding foot that encompasses the C-terminal cell interaction motif. We show that individual tropoelastin molecules are highly extensible yet elastic without hysteresis to perform as highly efficient molecular nanosprings. Our findings shed light on how biology uses this single protein to build durable elastic structures that allow for cell attachment to an appended foot. We present a unique model for head-to-tail assembly which allows for the propagation of the molecule's asymmetric coil through a stacked spring design.

Original languageEnglish (US)
Pages (from-to)4322-4327
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume108
Issue number11
DOIs
StatePublished - Mar 15 2011

Fingerprint

Tropoelastin
Elasticity
Elastin
Proteins
Foot
Elastic Tissue
Nanostructures
Neutrons
Cell Communication
Mammals
X-Rays

Keywords

  • AFM
  • Atomic force microscopy
  • SAXS

ASJC Scopus subject areas

  • General

Cite this

Shape of tropoelastin, the highly extensible protein that controls human tissue elasticity. / Baldock, Clair; Oberhauser, Andres; Ma, Liang; Lammie, Donna; Siegler, Veronique; Mithieux, Suzanne M.; Tu, Yidong; Chow, John Yuen Ho; Suleman, Farhana; Malfois, Marc; Rogers, Sarah; Guo, Liang; Irving, Thomas C.; Wess, Tim J.; Weiss, Anthony S.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 108, No. 11, 15.03.2011, p. 4322-4327.

Research output: Contribution to journalArticle

Baldock, C, Oberhauser, A, Ma, L, Lammie, D, Siegler, V, Mithieux, SM, Tu, Y, Chow, JYH, Suleman, F, Malfois, M, Rogers, S, Guo, L, Irving, TC, Wess, TJ & Weiss, AS 2011, 'Shape of tropoelastin, the highly extensible protein that controls human tissue elasticity', Proceedings of the National Academy of Sciences of the United States of America, vol. 108, no. 11, pp. 4322-4327. https://doi.org/10.1073/pnas.1014280108
Baldock, Clair ; Oberhauser, Andres ; Ma, Liang ; Lammie, Donna ; Siegler, Veronique ; Mithieux, Suzanne M. ; Tu, Yidong ; Chow, John Yuen Ho ; Suleman, Farhana ; Malfois, Marc ; Rogers, Sarah ; Guo, Liang ; Irving, Thomas C. ; Wess, Tim J. ; Weiss, Anthony S. / Shape of tropoelastin, the highly extensible protein that controls human tissue elasticity. In: Proceedings of the National Academy of Sciences of the United States of America. 2011 ; Vol. 108, No. 11. pp. 4322-4327.
@article{4f2ad5aac7c944319419cdabbcc29c12,
title = "Shape of tropoelastin, the highly extensible protein that controls human tissue elasticity",
abstract = "Elastin enables the reversible deformation of elastic tissues and can withstand decades of repetitive forces. Tropoelastin is the soluble precursor to elastin, the main elastic protein found in mammals. Little is known of the shape and mechanism of assembly of tropoelastin as its unique composition and propensity to self-associate has hampered structural studies. In this study, we solve the nanostructure of full-length and corresponding overlapping fragments of tropoelastin using small angle X-ray and neutron scattering, allowing us to identify discrete regions of the molecule. Tropoelastin is an asymmetric coil, with a protruding foot that encompasses the C-terminal cell interaction motif. We show that individual tropoelastin molecules are highly extensible yet elastic without hysteresis to perform as highly efficient molecular nanosprings. Our findings shed light on how biology uses this single protein to build durable elastic structures that allow for cell attachment to an appended foot. We present a unique model for head-to-tail assembly which allows for the propagation of the molecule's asymmetric coil through a stacked spring design.",
keywords = "AFM, Atomic force microscopy, SAXS",
author = "Clair Baldock and Andres Oberhauser and Liang Ma and Donna Lammie and Veronique Siegler and Mithieux, {Suzanne M.} and Yidong Tu and Chow, {John Yuen Ho} and Farhana Suleman and Marc Malfois and Sarah Rogers and Liang Guo and Irving, {Thomas C.} and Wess, {Tim J.} and Weiss, {Anthony S.}",
year = "2011",
month = "3",
day = "15",
doi = "10.1073/pnas.1014280108",
language = "English (US)",
volume = "108",
pages = "4322--4327",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "11",

}

TY - JOUR

T1 - Shape of tropoelastin, the highly extensible protein that controls human tissue elasticity

AU - Baldock, Clair

AU - Oberhauser, Andres

AU - Ma, Liang

AU - Lammie, Donna

AU - Siegler, Veronique

AU - Mithieux, Suzanne M.

AU - Tu, Yidong

AU - Chow, John Yuen Ho

AU - Suleman, Farhana

AU - Malfois, Marc

AU - Rogers, Sarah

AU - Guo, Liang

AU - Irving, Thomas C.

AU - Wess, Tim J.

AU - Weiss, Anthony S.

PY - 2011/3/15

Y1 - 2011/3/15

N2 - Elastin enables the reversible deformation of elastic tissues and can withstand decades of repetitive forces. Tropoelastin is the soluble precursor to elastin, the main elastic protein found in mammals. Little is known of the shape and mechanism of assembly of tropoelastin as its unique composition and propensity to self-associate has hampered structural studies. In this study, we solve the nanostructure of full-length and corresponding overlapping fragments of tropoelastin using small angle X-ray and neutron scattering, allowing us to identify discrete regions of the molecule. Tropoelastin is an asymmetric coil, with a protruding foot that encompasses the C-terminal cell interaction motif. We show that individual tropoelastin molecules are highly extensible yet elastic without hysteresis to perform as highly efficient molecular nanosprings. Our findings shed light on how biology uses this single protein to build durable elastic structures that allow for cell attachment to an appended foot. We present a unique model for head-to-tail assembly which allows for the propagation of the molecule's asymmetric coil through a stacked spring design.

AB - Elastin enables the reversible deformation of elastic tissues and can withstand decades of repetitive forces. Tropoelastin is the soluble precursor to elastin, the main elastic protein found in mammals. Little is known of the shape and mechanism of assembly of tropoelastin as its unique composition and propensity to self-associate has hampered structural studies. In this study, we solve the nanostructure of full-length and corresponding overlapping fragments of tropoelastin using small angle X-ray and neutron scattering, allowing us to identify discrete regions of the molecule. Tropoelastin is an asymmetric coil, with a protruding foot that encompasses the C-terminal cell interaction motif. We show that individual tropoelastin molecules are highly extensible yet elastic without hysteresis to perform as highly efficient molecular nanosprings. Our findings shed light on how biology uses this single protein to build durable elastic structures that allow for cell attachment to an appended foot. We present a unique model for head-to-tail assembly which allows for the propagation of the molecule's asymmetric coil through a stacked spring design.

KW - AFM

KW - Atomic force microscopy

KW - SAXS

UR - http://www.scopus.com/inward/record.url?scp=79952721821&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79952721821&partnerID=8YFLogxK

U2 - 10.1073/pnas.1014280108

DO - 10.1073/pnas.1014280108

M3 - Article

VL - 108

SP - 4322

EP - 4327

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 11

ER -