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Structural and physical basis for the elasticity of elastin

Published online by Cambridge University Press:  19 March 2024

Camille Depenveiller Open the ORCID record for Camille Depenveiller [Opens in a new window] ,
Stéphanie Baud Open the ORCID record for Stéphanie Baud [Opens in a new window] ,
Nicolas Belloy Open the ORCID record for Nicolas Belloy [Opens in a new window] ,
Brigida Bochicchio Open the ORCID record for Brigida Bochicchio [Opens in a new window] ,
Jany Dandurand Open the ORCID record for Jany Dandurand [Opens in a new window] ,
Manuel Dauchez Open the ORCID record for Manuel Dauchez [Opens in a new window] ,
Antonietta Pepe Open the ORCID record for Antonietta Pepe [Opens in a new window] ,
Régis Pomès Open the ORCID record for Régis Pomès [Opens in a new window] ,
Valérie Samouillan Open the ORCID record for Valérie Samouillan [Opens in a new window]  and
Laurent Debelle Open the ORCID record for Laurent Debelle [Opens in a new window]
Camille Depenveiller
Affiliation:
UMR URCA/CNRS 7369, Matrice Extracellulaire et Dynamique Cellulaire (MEDyC), UFR Sciences Exactes et Naturelles, SFR CAP Santé, Université de Reims Champagne-Ardenne, Reims, France Unité de Génie Enzymatique et Cellulaire UMR 7025 CNRS, Université de Picardie Jules Verne, Amiens, France
Stéphanie Baud
Affiliation:
UMR URCA/CNRS 7369, Matrice Extracellulaire et Dynamique Cellulaire (MEDyC), UFR Sciences Exactes et Naturelles, SFR CAP Santé, Université de Reims Champagne-Ardenne, Reims, France
Nicolas Belloy
Affiliation:
UMR URCA/CNRS 7369, Matrice Extracellulaire et Dynamique Cellulaire (MEDyC), UFR Sciences Exactes et Naturelles, SFR CAP Santé, Université de Reims Champagne-Ardenne, Reims, France
Brigida Bochicchio
Affiliation:
Laboratory of Bioinspired Materials, Department of Science, University of Basilicata, Potenza, Italy
Jany Dandurand
Affiliation:
CIRIMAT UMR 5085, Université Paul Sabatier, Université de Toulouse, Toulouse, France
Manuel Dauchez
Affiliation:
UMR URCA/CNRS 7369, Matrice Extracellulaire et Dynamique Cellulaire (MEDyC), UFR Sciences Exactes et Naturelles, SFR CAP Santé, Université de Reims Champagne-Ardenne, Reims, France
Antonietta Pepe
Affiliation:
Laboratory of Bioinspired Materials, Department of Science, University of Basilicata, Potenza, Italy
Régis Pomès
Affiliation:
Molecular Medicine, Hospital for Sick Children, Toronto, ON, Canada Department of Biochemistry, University of Toronto, Toronto, ON, Canada
Valérie Samouillan
Affiliation:
CIRIMAT UMR 5085, Université Paul Sabatier, Université de Toulouse, Toulouse, France
Laurent Debelle*
Affiliation:
UMR URCA/CNRS 7369, Matrice Extracellulaire et Dynamique Cellulaire (MEDyC), UFR Sciences Exactes et Naturelles, SFR CAP Santé, Université de Reims Champagne-Ardenne, Reims, France
*
Corresponding author: Laurent Debelle; Email: laurent.debelle@univ-reims.fr
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Abstract

Elastin function is to endow vertebrate tissues with elasticity so that they can adapt to local mechanical constraints. The hydrophobicity and insolubility of the mature elastin polymer have hampered studies of its molecular organisation and structure-elasticity relationships. Nevertheless, a growing number of studies from a broad range of disciplines have provided invaluable insights, and several structural models of elastin have been proposed. However, many questions remain regarding how the primary sequence of elastin (and the soluble precursor tropoelastin) governs the molecular structure, its organisation into a polymeric network, and the mechanical properties of the resulting material. The elasticity of elastin is known to be largely entropic in origin, a property that is understood to arise from both its disordered molecular structure and its hydrophobic character. Despite a high degree of hydrophobicity, elastin does not form compact, water-excluding domains and remains highly disordered. However, elastin contains both stable and labile secondary structure elements. Current models of elastin structure and function are drawn from data collected on tropoelastin and on elastin-like peptides (ELPs) but at the tissue level, elasticity is only achieved after polymerisation of the mature elastin. In tissues, the reticulation of tropoelastin chains in water defines the polymer elastin that bears elasticity. Similarly, ELPs require polymerisation to become elastic. There is considerable interest in elastin especially in the biomaterials and cosmetic fields where ELPs are widely used. This review aims to provide an up-to-date survey of/perspective on current knowledge about the interplay between elastin structure, solvation, and entropic elasticity.

Keywords

elasticityelastinentropymodelstructurewater

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Review
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Quarterly Reviews of Biophysics , Volume 57 , 2024 , e3
Copyright
© The Author(s), 2024. Published by Cambridge University Press

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