1947-37-1Relevant articles and documents
Enzymatic C-terminal amidation of amino acids and peptides
Nuijens, Timo,Piva, Elena,Kruijtzer, John A.W.,Rijkers, Dirk T.S.,Liskamp, Rob M.J.,Quaedflieg, Peter J.L.M.
experimental part, p. 3777 - 3779 (2012/09/22)
Herein, we describe two versatile and high yielding enzymatic approaches for the conversion of semi-protected amino acid and peptidyl C-terminal α-carboxylic acids into their corresponding amides. In the first approach, the lipase Candida antarctica lipase-B (Cal-B), and in the second approach, the protease Subtilisin A, are used, respectively. We found that by using the ammonium salt of the α-carboxylic acid instead of separate ammonia sources, the enzymatic amidation reactions proceeded much faster without side reactions and gave near to quantitative yields of products.
A Modified Benzhydrylamine as a Handle Reagent for the Solid Phase Synthesis of Peptide Amides Based on the Fluorenylmethoxycarbonyl Method
Funakoshi, Susumu,Murayama, Eigoro,Guo, Lili,Fujii, Nobutaka,Yajima, Haruaki
, p. 382 - 384 (2007/10/02)
An easily preparable dimethoxybenzhydrylamine derivative, 3-(α-Fmoc-amino-4-methoxybenzyl)-4-methoxyphenyl propionic acid (Fmoc=fluoren-9-ylmethoxycarbonyl) is a useful precursor of the C-terminal amide, when applied to Fmoc-based solid phase peptide synthesis; as a cleavage reagent from the resine, thioanisole-mediated trimethylsilyl bromide in trifluoroacetic acid is recommended.
Alternative Synthesis of the Carboxyl Terminal Tetrapeptide Amide of Cholecystokinin by Means of Proteases
Sakina, Kiyoshi,Kawazura, Keiko,Morihara, Kazuyuki
, p. 1717 - 1718 (2007/10/02)
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