The Biological Stability of β-Peptides: No Interactions between α- and β-Peptidic Structures?
Author(s) -
Tobias Hintermann,
Dieter Seebàch
Publication year - 1997
Publication title -
chimia international journal for chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.387
H-Index - 55
eISSN - 2673-2424
pISSN - 0009-4293
DOI - 10.2533/chimia.1997.244
Subject(s) - peptide , chemistry , amino acid , enzyme , degradation (telecommunications) , biochemistry , combinatorial chemistry , computer science , telecommunications
The use of peptides in pharmaceutical applications is always hindered by the rapid degradation of the peptides by enzymes. Recent work on β-peptides, peptides constructed entirely from β-amino acids, has shown that even the short-chain oligomers (6 or 7 residues) exhibit remarkably stable secondary structures. However, before certain applications of β-peptides can be considered, an information about their possible interactions or reactions with enzymes must be acquired.Ames tests (all negative) have now been performed on a selection of β-amino acids, which would be the result of the enzymatic degradation of a β-peptide. Furthermore, digestion experiments using a variety of peptidases and β-peptides have now shown that β-peptides, in sharp contrast to their α-peptide counterparts, undergo no degradation.
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