A strong positive dendritic effect in a peptide dendrimer-catalyzed ester hydrolysis reaction.
The contribution of the dendritic structure in catalysis of ester hydrolysis was investigated with a systematic peptide dendrimer series of increasing generation number (G1-G4) containing a catalytic consensus sequence His-Ser in all branches. A strong positive dendritic effect was observed with up to 100-fold increased histidine reactivity between G1 and G4. Kinetic studies and isothermal calorimetric titration experiments showed that the strong positive dendritic effect resulted from cooperativity between binding and catalysis.
Delort
Estelle
E
Department of Chemistry and Biochemistry, University of Berne, Freiestrasse 3, 3012 Berne, Switzerland.
Darbre
Tamis
T
Reymond
Jean-Louis
JL
D002151:Calorimetry / Q000379:methods; D002384:Catalysis; D004952:Esters / Q000737:chemistry*; D006639:Histidine / Q000737:chemistry*; D006868:Hydrolysis; D057927:Hydrophobic and Hydrophilic Interactions; D007093:Imidazoles / Q000737:chemistry; D007700:Kinetics; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*
D004952:Esters; D007093:Imidazoles; D010455:Peptides; D006639:Histidine; C023439:4-methylimidazole