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Conformational and thermal characterization of a synthetic peptidic fragment inspired from human tropoelastin: Signature of the amyloid fibers

Dandurand, Jany and Samouillan, Valérie and Lacoste-Ferré, Marie-Hélène and Lacabanne, Colette and Bochicchio, Brigida and Pepe, Antonietta Conformational and thermal characterization of a synthetic peptidic fragment inspired from human tropoelastin: Signature of the amyloid fibers. (2014) Pathologie Biologie, 62 (2). 100-107. ISSN 0369-8114

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Official URL: http://dx.doi.org/10.1016/j.patbio.2014.02.001


Objectives : This work deals with the conformational and thermal characterization of a synthetic peptide (S4) released during the proteolysis of human tropoelastin by the matrix metalloproteinase-12 that was shown to form amyloid-like fibres under certain conditions. Materials and methods : S4 peptides were synthesized by solid-phase methodology and aggregated in solution at 80 8C. Fourier transform–infrared spectroscopy (FT–IR) was used to access the secondary structure. Thermal characterization was performed by thermogravimetric analysis (TGA) and differential scanning calorimetry (DSC). Results : The DSC study of the soluble linear peptide S4 in solution in TBS reveals the irreversible aggregation into amyloid fibres. FT–IR, DSC and TGA analyses performed on freeze-dried samples evidence differences between the linear peptide and its associated amyloid-like fibres, both on the conformation and the physical structure. When S4 peptides are aggregated, the prominent conformation scanned by FT–IR is the cross b-structure, corresponding to TGA to an increase of the thermal stability. Moreover, the DSC thermograms of S4 fibres are characteristic of a highly ordered structure, in contrast to the DSC thermograms of S4 linear peptides, characteristic of an amorphous structure. Finally, the DSC analysis of differently hydrated S4 fibres brings to the fore the specific thermal answer of the wet interfaces of the cross b-fibres. Conclusion : FT–IR and thermal techniques are well suited to evidence conformational and structural differences between the soluble peptide and its amyloid form.

Item Type:Article
Additional Information:Thanks to Elsevier editor. The definitive version is available at http://www.sciencedirect.com The original PDF of the article can be found at Pathologie Biologie website : http://www.sciencedirect.com/science/article/pii/S0369811414000212
HAL Id:hal-00980025
Audience (journal):International peer-reviewed journal
Uncontrolled Keywords:
Institution:French research institutions > Centre National de la Recherche Scientifique - CNRS (FRANCE)
Université de Toulouse > Institut National Polytechnique de Toulouse - Toulouse INP (FRANCE)
Université de Toulouse > Université Toulouse III - Paul Sabatier - UT3 (FRANCE)
Other partners > Università degli Studi della Basilicata - UNIBAS (ITALY)
Laboratory name:
Deposited On:17 Apr 2014 09:32

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