Authors: Samouillan, Valerie¹; Lamure, Alain¹; Maurel, Eliane¹; Dandurand, Jany¹; Lacabanne, Colette¹; Spina, Michel²

Source: Journal of Biomaterials Science, Polymer Edition, Volume 11, Number 6, 2000 , pp. 583-598(16)

Publisher: VSP, an imprint of Brill

Abstract:

The low temperature dielectric relaxation of porcine aortic valves and its main macromolecular proteins, i.e. elastin and collagen, have been investigated in the dry state and at low levels of hydration by thermally stimulated currents spectrometry, with an equivalent frequency of 10-3 Hz. Two secondary relaxation modes, labeled γ and β with increasing temperature, are found for the three materials. Since the γ-mode is independent upon hydration while the β-mode is strongly plasticized by water, these relaxation modes have been attributed to localized motions of the polypeptidic chains containing apolar and polar residues, respectively. The deconvolution of the β-mode by fractional polarization gives the experimental distribution of the dielectric relaxation times of the three materials, and allows us to deduce the activation parameters of each elementary process. These analyses shows the existence of compensation phenomena between the activation parameters, implying cooperative mechanisms. The occurrence of these phenomena with their characteristic parameters are used to specify the origin of the localized relaxation modes in collagen and elastin, and to assign the specific role of each protein in the aortic valves.

Keywords: ELASTIN; COLLAGEN; AORTIC; VALVES; THERMALLY; STIMULATED; CURRENTS; DIELECTRIC; RELAXATIONS; LOCALIZED; MOTIONS

Document Type: Research article

DOI: http://dx.doi.org/10.1163/156856200743887

Affiliations: 1: Laboratoire de Physique des Polymères, Université Paul Sabatier, 31062 Toulouse Cedex, France 2: Istituto di Istologia, Universita degli Studi di Padova, 35121 Padova, Italy

Publication date: 2000-07-30

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• In this Subject: Chemistry (General) ,  Engineering/Technology ,  Materials & Manufacturing
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