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Circular dichroism and electron microscopy studies in vitro of 33-mer gliadin peptide revealed secondary structure transition and supramolecular organization
Version of Record online: 25 OCT 2013
Copyright © 2013 Wiley Periodicals, Inc.
Volume 101, Issue 1, pages 96–106, January 2014
How to Cite
Herrera, M. G., Zamarreño, F., Costabel, M., Ritacco, H., Hütten, A., Sewald, N. and Dodero, V. I. (2014), Circular dichroism and electron microscopy studies in vitro of 33-mer gliadin peptide revealed secondary structure transition and supramolecular organization. Biopolymers, 101: 96–106. doi: 10.1002/bip.22288
- Issue online: 25 OCT 2013
- Version of Record online: 25 OCT 2013
- Accepted manuscript online: 22 MAY 2013 11:15AM EST
- Manuscript Accepted: 9 MAY 2013
- Manuscript Revised: 7 MAY 2013
- Manuscript Received: 29 JAN 2013
- CONICET (National Scientific and Technical Research Council), ANCyPT (National Agency for Promotion of Science and Technology), UNS (Universidad Nacional del Sur), and DAAD (German Academic Exchange Service)
Additional Supporting Information may be found in the online version of this article.
Figure S1. Concentrationdependence experiments of 33 mer in water, pH 7.0: 46 μM (○), 93μM (□) , 197 μM (•), 317 µM(♦) ,317 µM (▪), 418 (◊), 613µM (♦).
Figure S2. Control Electron micrograph of 1 mM sodium citrate, 1 mM sodium borate, 1 mM sodium phosphate buffer, 15 mM NaCl, pH 7.0 (A) TEM micrographs. (B) SEM micrographs. The brightness observed is characteristics of inorganic salts
Figure S3.(A) SEM micrograph of 33-mer peptide in water, pH 7.0. (B) Fibrils diameter distribution showing the presence of two kind of them, one of 53nm and other of 86 nm .
Figure S4. HPLC report of 33-mer gliadin peptide
Figure S5. ESI-Mass Spectra of 33-mer gliadin peptide
Figure S6. Accurate-Mass-determination
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