3249-01-2Relevant articles and documents
One-step C-terminal deprotection and activation of peptides with peptide amidase from stenotrophomonas maltophilia in neat organic solvent
Arif, Muhammad I.,Toplak, Ana,Szymanski, Wiktor,Feringa, Ben L.,Nuijens, Timo,Quaedflieg, Peter J. L. M.,Wu, Bian,Janssen, Dick B.
, p. 2197 - 2202 (2014/07/21)
Chemoenzymatic peptide synthesis is a rapidly developing technology for cost effective peptide production on a large scale. As an alternative to the traditional C→N strategy, which employs expensive N-protected building blocks in each step, we have investigated an N→C extension route that is based on activation of a peptide C-terminal amide protecting group to the corresponding methyl ester. We found that this conversion is efficiently catalysed by Stenotrophomonas maltophilia peptide amidase in neat organic media. The system excludes the possibility of internal peptide cleavage as the enzyme lacks intrinsic protease activity. The produced peptide methyl ester was used for peptide chain extension in a kinetically controlled reaction by a thermostable protease.
PLURIPOTENTIAL AMINO ACIDS I. (L)-p-DIHYDROXYBORYLPHENYLALANINE (L-Bph) AS A PRECURSOR OF L-Phe AND L-Tyr CONTAINING PEPTIDES; SPECIFIC TRITIATION OF L-Phe-CONTAINING PEPTIDES AT A FINAL STEP IN THE SYNTHESIS
Roberts, David C.,Suda, Kohji,Samanen, James,Kemp, D. S.
, p. 3435 - 3438 (2007/10/02)
p-Dihydroxyborylphenylalanine has been resolved and incorporated into simple di and tripeptides; treatment of these with hydrogen peroxide or diammino silver salts results respectively in formation of tyrosine and phenylalanine peptides.
Amino-acids and peptides. XXIV. The use of esters of 1-hydroxypiperidine and of other NN-dialkylhydroxylamines in peptide synthesis and as selective acylating agents.
Handford,Jones,Young,Johnson
, p. 6814 - 6827 (2007/10/04)
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