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Rotaxane‐Based Propeptides: Protection and Enzymatic Release of a Bioactive Pentapeptide
Author(s) -
Fernandes Anthony,
Viterisi Aurélien,
Coutrot Frédéric,
Potok Stéphanie,
Leigh David A.,
Aucagne Vincent,
Papot Sébastien
Publication year - 2009
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.200903215
Subject(s) - pentapeptide repeat , rotaxane , peptide , chemistry , cleavage (geology) , enzyme , polycaprolactone , biochemistry , biology , polymer , organic chemistry , molecule , supramolecular chemistry , fracture (geology) , paleontology
Ring of protection : A [2]rotaxane 1 protects and selectively releases a bioactive pentapeptide. The rotaxane macrocycle provides a defensive shield that very significantly improves the poor stability of the peptide to both individual peptidases and the cocktail of enzymes present in human plasma. Glycosidase‐catalyzed cleavage of a carbohydrate ‘stopper’ in the rotaxane triggers release of the parent peptide (see picture).