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Water structure and elastin-like peptide aggregation

Dandurand, Jany and Samouillan, Valérie and Lacabanne, Colette and Pepe, Antonietta and Bochicchio, Brigida Water structure and elastin-like peptide aggregation. (2014) Journal of Thermal Analysis and Calorimetry. 1-8. ISSN 1388-6150

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Official URL: http://dx.doi.org/10.1007/s10973-014-4254-9

Abstract

For the first time, calorimetric studies performed at very low temperature highlighted the preliminary and required conditions for further aggregation/coacervation of peptides from elastin in solution through the structural water reorganization around the peptides. For this purpose, we firstly characterized by turbidimetry and differential scanning calorimetry the synthetic S4 fragment peptide containing the XGGZG motif (where X and Z correspond to Valine or Leucine) which is able to form amyloid fibres under certain conditions. We also investigated two mediumsized elastin-related model elastin peptides containing the VGVPG motif (E50 and E18) as well as their analogues where proline is hydroxylated in hydroxyproline. These peptides were shown to coacervate, and a close correlation was found between the inverse transition temperature obtained by turbidimetry and the clathrate-like structures evidenced at low temperature by the calorimetric method.

Item Type:Article
Additional Information:Thanks to Springer editor. The definitive version is available at http://link.springer.com/article/10.1007%2Fs10973-014-4254-9
HAL Id:hal-01108635
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 - INPT (FRANCE)
Université de Toulouse > Université Toulouse III - Paul Sabatier - UPS (FRANCE)
Other partners > Università degli Studi della Basilicata - UNIBAS (ITALY)
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Deposited By: cirimat webmestre
Deposited On:23 Jan 2015 10:28

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