70897-15-3Relevant 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.
Derivatives of antibiotic GE2270 factors C2a, D2 and E
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, (2008/06/13)
Mono- or di-substituted derivatives of GE2270 factors C2a, D2 and E of general formula (I), wherein W represents a moiety of formula (a), (b) or (c), R1 and R2 representing a variety of substituents, X1 is methyl, X2 is a --CH2 --W1 moiety and X3 is methylamino or amino, or X1 is a --CH2 --W1 moiety, X2 is methoxymethylene and X3 is methylamino, with the proviso that when X3 is amino, then W must be 2-(aminocarbonyl)-pyrrolidinyl; with the further proviso that when W is 2-(aminocarbonyl)-pyrrolidinyl, then W1 cannot be hydroxy; and the pharmaceutically acceptable salts thereof. The mono- or di-substituted derivatives of antibiotic GE 2270 of formula (I) are antimicrobial agents mainly active against gram positive bacteria. STR1
Biologically active peptides, processes for preparing them and pharmaceutical compositions
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, (2008/06/13)
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