Water dependent structural changes of silk from Bombyx mori gland to fibre as evidenced by Raman and IR spectroscopies |
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| Institution: | 1. Sorbonne Universités, UPMC Univ. Paris 06, UMR 8233, MONARIS, F-75005 Paris, France;2. CNRS, UMR 8233, MONARIS, F-75005 Paris, France;3. Biologie Fonctionnelle, Insectes et Interaction (bf2i), INRA/INSA, 69621 Villeurbanne Cedex, France;1. Sorbonne Universités, Paris, France;2. UMR BOREA, Biologie des Organismes et des Ecosystèmes Aquatiques, UMR MNHN/CNRS 7208/UPMC/UCN/UA/IRD 207, Muséum National d’Histoire Naturelle, 75005 Paris, France;3. ID21, European Synchrotron Radiation Facility, 38000 Grenoble, France;4. Central Facility for Electron Microscopy, University of Ulm, 89069 Ulm, Germany;5. UMR MONARIS, De la Molécule aux Nano-Objets: Réactivité, Interactions et Spectroscopies, UMR 8233 CNRS-Université Pierre et Marie Curie, 75005 Paris, France;6. Institut de Systématique, Evolution, Biodiversité, Muséum National d’Histoire Naturelle, 75005 Paris, France;1. Institute of Archaeology, Knez Mihailova 35/IV, 11000 Belgrade, Serbia;2. National Museum in Belgrade, Trg Republike 1a, 11000 Belgrade, Serbia;3. Faculty of Technology, University of Novi Sad, Bulevar Cara Lazara 1, 21000 Novi Sad, Serbia;1. Department of Bioengineering, Faculty of Engineering, Ege University, 35100 Bornova, Izmir, Turkey;2. Department of Genetic & Bioengineering, Faculty of Engineering, Gumushane University, 29100 Gumushane, Turkey;3. Hamburg University of Technology, Institute of Thermal Separation Processes, Eißendorferstr. 38, D 21073 Hamburg, Germany;4. Hamburg University of Technology, Institute of Microsystems Technology, Eißendorferstr. 42, M 21073 Hamburg, Germany;1. Bozok University, Faculty of Arts and Sciences, Department of Chemistry, Yozgat, Turkey;2. Erciyes University, Faculty of Sciences, Department of Chemistry, Kayseri, Turkey |
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| Abstract: | DSC, attenuated total reflexion infrared (ATR-FTIR), and Raman microspectroscopy were used for the first time in a close to in vivo environment to study ready-to-spin Bombyx mori silkworms. The aim was to understand the change of the fibroin backbone organisation from the gland to the fibre. Raman shifts of the Amide I components reveal a strong change of organisation in the middle part of the hydrated gland, as anticipated previously measured modifications of salts concentrations and pH. Series of bands characteristics of the fully hydrated silk disappear, as observed for spider silk, despite the different aminoacid sequence. Confirmation is obtained from IR spectra taking into account the superimposed water component. The change of the silk–water interaction in the central part of the gland, from a hydrophobic to hydrophilic behaviour, is related to the water content decrease along the gland. pH sensitive carboxylate side chains markers confirm the modification. Fibroin organisation was also studied in the dried gland and in the spun fibre. The fibre extrusion by orients the fibroin chains along the fibre axis, with intercalated water molecules, leading to a material with specific mechanical properties, compared to the amorphous dried gland. |
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| Keywords: | Silk Gland Fibre Conformation Water Raman ATR-FTIR |
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