Synthesis of α-fluoroalkyl substituted peptides via enzymatic fragment condensation

A peptide library consisting of di- and tripeptide esters and tripeptide amides, respectively, containing α-Tfm amino acids in different positions was synthesized and tested for enzymatic fragment condensations catalyzed by the proteases α-chymotrypsin, trypsin and clostripain.

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Bibliographic Details
Published inTetrahedron: asymmetry Vol. 10; no. 2; pp. 307 - 313
Main Authors Bordusa, Frank, Dahl, Christina, Jakubke, Hans-Dieter, Burger, Klaus, Koksch, Beate
Format Journal Article
LanguageEnglish
Published OXFORD Elsevier Ltd 29.01.1999
Elsevier
Subjects
Chemistry
Chemistry, Inorganic & Nuclear
Chemistry, Organic
Chemistry, Physical
Physical Sciences
Science & Technology
CHYMOTRYPSIN
SPECIFICITY
AMINO-ACIDS
ACYL TRANSFER
BOND
DERIVATIVES
CLOSTRIPAIN
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Summary:A peptide library consisting of di- and tripeptide esters and tripeptide amides, respectively, containing α-Tfm amino acids in different positions was synthesized and tested for enzymatic fragment condensations catalyzed by the proteases α-chymotrypsin, trypsin and clostripain.
ISSN:0957-4166
1362-511X
DOI:10.1016/S0957-4166(98)00508-4