53907-19-0Relevant academic research and scientific papers
Peptide Synthesis by Prior Thiol Capture. 6. Rates of the Disulfide Bond Forming Capture Reaction and Demonstration of the Overall Strategy by Synthesis of the C-Terminal 29-Peptide Sequence of BPTI
Fotouhi, Nader,Galakatos, Nicholas George,Kemp, D. S.
, p. 2803 - 2817 (2007/10/02)
Peptide bond formation by prior thiol capture involves as a first step formation of a disulfide bond between two S-functionalized peptide fragments, one bearing a 4-(acyloxy)-6-mercaptodibenzofuran at its C-terminus, the other bearing an S-activated cysteine residue at its N-terminus.The Scm procedure (Scm MeO-CO-S) of Brois and others is used to generate disulfides of general structure -Cys(S-S-Ar)- by reaction of suitable arene thiols with -Cys(S-Scm)- derivatives.Mixtures of hexafluoroisopropyl alcohol (HFIP) with water and acetonitrile facilitate this reaction, which is markedly accelerated by traces of tertiary amines, by electron-withdrawing groups near the Scm function, and by an increase in the fraction of water in the mixture.A 94percent yield in 5 min was seen for reaction of the trifluoroacetate salt of H-L-Cys(S-Scm)-OMe (5*10-4 M) with 4-mercaptodibenzofuran (5*10-4 M) in 9:1 HFIP-MeCN.The scope of the thiol capture strategy is demonstrated by a four-fragment, three-stage assembly of the 29-peptyde sequence 30-58 of the protein basic pancreatic trypsin inhibitor (BPTI).
