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Development and Biological Assessment of Fully Water‐Soluble Helical Aromatic Amide Foldamers
Author(s) -
Gillies Elizabeth R.,
Deiss Frédérique,
Staedel Cathy,
Schmitter JeanMarie,
Huc Ivan
Publication year - 2007
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200700301
Subject(s) - amide , chemistry , folding (dsp implementation) , aromatic amino acids , peptidomimetic , peptide , protease , combinatorial chemistry , biophysics , amino acid , organic chemistry , biochemistry , biology , electrical engineering , enzyme , engineering
Abiotic but bioactive : Folding aromatic amide oligomers possessing helical structures very different from those of α‐peptides, β‐peptides, or peptoids nevertheless show comparable abilities to penetrate into cells, as well as low toxicity and complete resistance to protease degradation. TFA − =trifluoroacetate.