title: Solid-state studies on synthetic fragments and analogues of elastin.
abstract: A series of synthetic fragments and analogues of elastin have been investigated, in the solid state, by means of differential scanning calorimetry and thermally stimulated current. Most of the polypeptides were shown to possess both amorphous regions and segments of long-range order. Water, which interacts preferentially with the amorphous zones, behaves as plasticizer, i.e. facilitates the localized motions of polypeptide chains. The results obtained have been correlated with elastin elasticity, in particular as far as the fundamental destructuring role of water is concerned.
authors.affiliation: Pierre Fabre Medicaments, Castres, France.
authors.forename: C
authors.initials: C
authors.lastname: Megret
authors.forename: A
authors.initials: A
authors.lastname: Lamure
authors.forename: M T
authors.initials: MT
authors.lastname: Pieraggi
authors.forename: C
authors.initials: C
authors.lastname: Lacabanne
authors.forename: V
authors.initials: V
authors.lastname: Guantieri
authors.forename: A M
authors.initials: AM
authors.lastname: Tamburro
mesh_terms: D000595:Amino Acid Sequence; D002152:Calorimetry, Differential Scanning; D004549:Elastin / Q000031:analogs & derivatives / Q000138:chemical synthesis / Q000737:chemistry*; D004560:Electricity; D006358:Hot Temperature; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry*; D011489:Protein Denaturation; D014867:Water
chemical_list: D009842:Oligopeptides; D010446:Peptide Fragments; D014867:Water; D004549:Elastin