86895-14-9Relevant articles and documents
Site-selective chemical cleavage of peptide bonds
Elashal, Hader E.,Raj, Monika
supporting information, p. 6304 - 6307 (2016/05/24)
Site-selective cleavage of extremely unreactive peptide bonds is a very important chemical modification that provides invaluable information regarding protein sequence, and it acts as a modulator of protein structure and function for therapeutic applications. For controlled and selective cleavage, a daunting task, chemical reagents must selectively recognize or bind to one or more amino acid residues in the peptide chain and selectively cleave a peptide bond. Building on this principle, we have developed an approach that utilizes a chemical reagent to selectively modify the serine residue in a peptide chain and leads to the cleavage of a peptide backbone at the N-terminus of the serine residue. After cleavage, modified residues can be converted back to the original fragments. This method exhibits broad substrate scope and selectively cleaves various bioactive peptides with post-translational modifications (e.g. N-acetylation and -methylation) and mutations (d- and β-amino acids), which are a known cause of age related diseases.
Synthesis of ureidopeptides using pentafluorophenyl carbamates from N a-Fmoc-peptide acids
Sureshbabu, Vommina V.,Venkataramanarao, Rao
, p. 910 - 919 (2008/12/23)
Highly active and shelf stable pentafluoro phenol derived Fmoc-peptidyl carbamates have been synthesized from corresponding Fmoc-peptidyl isocyanates. The utility of pentafluorophenyl carbamate intermediates has been demonstrated by the synthesis of tri, penta and hexapeptidyl ureas which are obtained in good yields. All the synthesised compounds have been characterized by 1H NMR, 13C NMR and mass spectroscopy. The coupling reaction using pentafluorophenyl carbamates to insert urea bond between α amino acids is fast, clean and high yielding.
SYNTHESIS OF HUMAN M BLOOD GROUP ANTIGENIC GLYCOPEPTIDE
Nakahara, Yoshiaki,Iijima, Hiroyuki,Ogawa, Tomoya
, p. 3321 - 3324 (2007/10/02)
A first total synthesis of terminal glycoheptapeptide of human glycophorin AM was accomplished by solution phase peptide condensation utilizing the tetrasaccharide-linked amino acid building blocks designed for Fmoc strategy.
