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Internalization of a Peptide into Multilamellar Vesicles Assisted by the Formation of an α‐Oxo Oxime Bond
Author(s) -
Richard Antoine,
BourelBonnet Line
Publication year - 2005
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.200500480
Subject(s) - internalization , oxime , vesicle , peptide , bond , chemistry , peptide bond , stereochemistry , business , organic chemistry , biochemistry , membrane , finance , cell
Abstract As part of a drug‐delivery project, we designed and synthesised a novel hydroxylamine cholesterol‐based anchor to ensure the chemoselective ligation of recognition patterns onto multilamellar vesicles by oxime ligation. The entry of a glyoxylyl peptide into the vesicles was unexpectedly assisted by the formation of the α‐oxo oxime bond. We studied extensively the kinetic and thermodynamic aspects of this phenomenon. Briefly, for a glyoxylyl peptide, the speed and ability to enter the vesicle were dependent upon 1) the presence of a hydroxylamine anchor of the type CholE 3 ONH 2 , 2) the amount of peptide engaged in the ligation and 3) the flip‐flop motion permitted by the different formulations, in which the presence of cholesterol seems to play an important role.