title: N-lipidated oligopeptides immobilized on cellulose as new type of organocatalysts.
abstract: A library of supramolecular structures formed by self-organization of N-lipidated tripeptides, dipeptides and N-acylated amino acids attached to cellulose according to the TASP concept via aminophenylamino-1,3,5-triazine was synthesized and the catalytic activity of the structures was studied. Intensive catalytic activity in solvolysis of sterically hindered Z-Aib-Aib-ONp under ambient conditions was observed for structures bearing the catalytic triad as well as for structures with the peptide fragment shortened to a dipeptide or even a single Ser, Glu or His residue, but not for structures bearing alanine or phenylalanine residues. For all structures with a dipeptide or a single amino acid residue and for most of tripeptide structures the progress of solvolysis was stopped after the concentration of the nitrophenolate ion reached 0.5-0.7 x 10-4 M/L. Only in the case of catalysts with glutamic acid residues in the tripeptide fragment, solvolysis proceeded until all the substrate was consumed.
authors.affiliation: Institute of Organic Chemistry, Technical University of Lodz, Zeromskiego116, 90-924 Lodz, Poland.
authors.forename: Justyna
authors.initials: J
authors.lastname: Fraczyk
authors.forename: Beata
authors.initials: B
authors.lastname: Kolesinska
authors.forename: Zbigniew J
authors.initials: ZJ
authors.lastname: Kaminski
mesh_terms: D002236:Carbohydrate Conformation; D002384:Catalysis; D002482:Cellulose / Q000737:chemistry*; D008055:Lipids / Q000737:chemistry*; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry*
chemical_list: D008055:Lipids; D009842:Oligopeptides; D002482:Cellulose