The structures of elastins and their function

Citation
L. Debelle et Ajp. Alix, The structures of elastins and their function, BIOCHIMIE, 81(10), 1999, pp. 981-994
Citations number
87
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHIMIE
ISSN journal
03009084 → ACNP
Volume
81
Issue
10
Year of publication
1999
Pages
981 - 994
Database
ISI
SICI code
0300-9084(199910)81:10<981:TSOEAT>2.0.ZU;2-S
Abstract
Elastin structures and their significance towards elastic recoil properties have been reviewed. Starting from the initial hypothesis that elastin conf ormation is conditioned by that of its monomer, the structure of tropoelast in was first described using theoretical and experimental methods and a bet a class folding type was evidenced for the isolated unbound tropoelastin mo lecules. The structure of elastin in the solid state was consistent with th at of its monomer and consequently, fibrous elastin appeared constituted of globular tropoelastin molecules. Finally, theoretical and experimental con siderations have led us to the conclusion that the functional form of the e lastomer, water swollen elastin, could be a triphasic system comprising the protein chains, hydration water and solvent water. Following this descript ion, the dynamic structural equilibria occurring within elastin hydrophobic domains and the plastisizing effect of water could explain elastin elastic ity, in keeping with a classical entropic mechanism. (C) 1999 Societe franc aise de biochimie et biologie moleculaire / Editions scientifiques et medic ales Elsevier SAS.