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Figure 2

ID
ZDB-IMAGE-210825-18
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Figures for Melo et al., 2021
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Figure Caption

Figure 2

A spectrum obtained by circular dichroism. Circular dichroism was performed to determine the peptide interaction with chemically modified heparins, demonstrating an alteration in the secondary structure of this peptide. Porcine heparin (Hep), Heparin 2-O-sulfated and N-sulfated heparin (Hep2SNS), Heparin 6-O-sulfated and N-sulfated (Hep6SNS), Heparin 2-O-sulfated and 6-O-sulfated (Hep2S6S), Heparin 6-sulfated (Hep6S), Heparin 2-sulfated (Hep2S), and Heparin N-sulfated (HepNS). The heparins that showed the greatest interaction with the peptide were the molecules containing N-sulfation. The assay was performed in the presence of 12 µM of the HS binding peptide and 6.7 µg/ml of each heparin in a 10 mM sodium phosphate solution. Control, 12µM of peptide in 10mM sodium phosphate solution. (A) The lines represent the repeat averages of eight different experimental readings. (B) The percentage of right-twisted antiparallel beta-sheet was analyzed. A reduction from the right-twisted shape to the left-twisted or relaxed shape was observed specifically with N-sulfated heparins.

Acknowledgments
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