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. Author manuscript; available in PMC: 2016 Jun 15.
Published in final edited form as: Bioorg Med Chem. 2015 Mar 20;23(12):2761–2766. doi: 10.1016/j.bmc.2015.03.040

Figure 3.

Figure 3

The selenylsulfide-bridged peptide is resistant to the reducing effects of DTT. By circular dichroism analysis, the selenylsulfide showed a notable shift in the minimum from 201 nm to 198 nm after the addition of 400 μM DTT (32 equivalents), demonstrating the stability of the peptide in the presence of a reducing agent. The dashed line indicates the minima at 0 μM DTT.