Bovine Elastin and κ-Elastin Secondary Structure Determination by Optical Spectroscopies

Autor: Bernard Sombret, Laurent Debelle, Pierre Legrand, Jean-Pierre Huvenne, Alain J.P. Alix, Maurice Berjot, Marie-Paule Jacob
Přispěvatelé: Laboratoire de Spectroscopies et Structures Biomoléculaires (LSSBM) (EA3305), Centre National de la Recherche Scientifique (CNRS), Laboratoire de Recherche Vasculaire Translationnelle (LVTS (UMR_S_1148 / U1148)), Université Paris 13 (UP13)-Université Paris Diderot - Paris 7 (UPD7)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire Avancé de Spectroscopie pour les Intéractions la Réactivité et l'Environnement - UMR 8516 (LASIRE), Institut de Chimie du CNRS (INC)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Institut de Chimie du CNRS (INC)-Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Centrale Lille Institut (CLIL)
Jazyk: angličtina
Rok vydání: 1995
Předmět:
Zdroj: Journal of Biological Chemistry
Journal of Biological Chemistry, 1995, 270 (44), pp.26099-26103. ⟨10.1074/jbc.270.44.26099⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 1995, 270 (44), pp.26099-26103. ⟨10.1074/jbc.270.44.26099⟩
ISSN: 0021-9258
1083-351X
DOI: 10.1074/jbc.270.44.26099⟩
Popis: Elastin is the macromolecular polymer of tropoelastin molecules responsible for the elastic properties of tissues. The understanding of its specific elasticity is uncertain because its structure is still unknown. Here, we report the first experimental quantitative determination of bovine elastin secondary structures as well as those of its corresponding soluble kappa-elastin. Using circular dichroism and Fourier transform infrared and near infrared Fourier transform Raman spectroscopic data, we estimated the secondary structure contents of elastin to be approximately 10% alpha-helices, approximately 45% beta-sheets, and approximately 45% undefined conformations. These values were very close to those we had previously determined for the free monomeric tropoelastin molecule, suggesting thus that elastin would be constituted of a closely packed assembly of globular beta structural class tropoelastin molecules cross-linked to form the elastic network (liquid drop model of elastin architecture). The presence of a strong hydration shell is demonstrated for elastin, and its possible contribution to elasticity is discussed.
Databáze: OpenAIRE