1356006-89-7

Upstream product

• 71989-31-6 Fmoc-Pro-OH 
• 1278509-69-5 Cys-Phe-Arg-Ala-Asn-Lys-OH 
• 1356006-80-8 C₃₄H₅₃N₉O₉S 
• 15761-39-4 1-(tert-butoxycarbonyl)-L-proline 
• 13139-15-6 N-tert-butoxycarbonyl-L-leucine 
• 15761-38-3 L-N-Boc-Ala 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 13836-37-8 Boc-Arg(Tos)-OH 
• 54613-99-9 Boc-(S)-Lys(2-Cl-Z)-OH 
• 47689-67-8 (S)-3-[4-(2-Bromo-benzyloxycarbonyloxy)-phenyl]-2-tert-butoxycarbonylamino-propionic acid 
• 65420-40-8 (S)-2-tert-Butoxycarbonylamino-N-(9H-xanthen-9-yl)-succinamic acid 
• 1356006-84-2 C₃₁H₄₉N₉O₇Se 

Relevant academic research and scientific papers

Bis(2-sulfanylethyl)amido peptides enable native chemical ligation at proline and minimize deletion side-product formation

Native chemical ligation of C-terminal peptidyl prolyl alkylthioesters with N-terminal cysteinyl peptides usually exhibits poor kinetic rates compared to other C-terminal amino acid residues. It is shown here that the reaction is accompanied by the formation of a deletion side product which is minimized by using a bis(2-sulfanylethyl)amido (SEA) thioester surrogate at a mildly acidic pH.

Preformed selenoesters enable rapid native chemical ligation at intractable sites

Going pro: The first facile Pro-Cys ligation using a preformed prolyl selenoester is reported (see scheme; P=peptide). In a comparative study of peptide selenoesters in native chemical ligation peptide α-selenoesters are shown to be superior acyl donors and result in rate enhancements of at least two orders of magnitude when compared to the well-established peptide α-thioesters. This method permits rapid chemical ligation even at previously intractable sites, such as Pro-Cys. Copyright