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N-Lipidated Oligopeptides Immobilized on Cellulose as New Type of Organocatalysts

[ Vol. 16 , Issue. 7 ]

Author(s):

Justyna Fraczyk, Beata Kolesinska and Zbigniew J. Kaminski   Pages 562 - 571 ( 10 )

Abstract:


A library of supramolecular structures formed by self-organization of N-lipidated tripeptides, dipeptides and Nacylated 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.

Keywords:

Catalysis, chemzyme, organocatalysis, self-organization, supramolecular, α-methylalanine.

Affiliation:

Institute of Organic Chemistry, Technical University of Lodz, Zeromskiego116, 90-924 Lodz, Poland.



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