Hello all,
I am currently working on the regioselective folding of a three disulfide bond-containing peptide. The orthogonal protecting groups I used and deprotected in order were Trt, Acm, and Mob. I was expecting that the fully oxidized peptide would be a dominant peak with few minor side peaks on the HPLC chromatogram. However, the regioselective folding profile was identical to the air random oxidation. I suspected that it might be disulfide scrambling during the final selective oxidation process, but these two profiles still shouldn't be the same. Also, I couldn't find the reports about disulfide scrambling happened during oxidation without redox reagents, and it left me a lot of questions. If it is possible, I will appreciate any advice and suggestion.
Thank you.
Ray
Disulfide scrambling occurs mainly during heating. It is a reduction not oxidation process. However, it could happen in a parallel reaction. Remove the oxidant and keep the other parameters the same including temperature. you will have your answer.
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