Human tropoelastin sequence

Doris Tintar (1) , Valérie Samouillan (1) , Jany Dandurand (1) , Colette Lacabanne (1) , Antonietta Pepe (2) , Brigida Bochicchio (2) , Antonio Mario Tamburro (2)

1 CIRIMAT - Centre interuniversitaire de recherche et d'ingenierie des matériaux
2 UNIBAS - Università degli studi della Basilicata [Potenza]

Calorimetric studies were performed on exon 6 in powdered form and in solution [water and 2,2,2- trifluoroethanol (TFE), a structure-inducing solvent or cosolvent]. Dynamic dielectric spectroscopy (DDS) analyses were realized in water and 20% TFE. The major role of solvent–peptide organization is evidenced with these techniques. Calorimetric measurements reveal the structural water organization around the polypeptide as well as the presence of hydrophobic interactions in TFE solution. Dielectric measurements showed for exon 6/ water a decrease of relaxations times of bulk solvent implying a faster dynamics with a slight increase of the activation entropy, suggesting that exon 6 probably creates disorder within the solvent. For TFE/water mixtures, an influence of exon 6 on its environment was seen with a relaxation associated with the exon 6/solvent interactions reinforced by storage of 72 h. Finally, exon 6/solvent interactions were clearly observed with addition of TFE.

Mots clés: Dielectric spectroscopy; Thermal analysis; Elastin

Domaines: Matériaux et structures en mécanique [physics.class-ph]; Micro et nanotechnologies/Microélectronique

Doris Tintar, Valérie Samouillan, Jany Dandurand, Colette Lacabanne, Antonietta Pepe, et al.. Human tropoelastin sequence: Dynamics of polypeptide coded by exon 6 in solution. Biopolymers, 2009, 91 (11), pp.943-952. ⟨10.1002/bip.21282⟩. ⟨hal-03474818⟩