Screening of a combinatorial library reveals peptide-based catalysts for phosphorester cleavage in water.
A combinatorial library of 625 octapeptides was screened for their efficiency to catalyze phosphorester cleavage in water. Octapeptides such as 1c, which contains a catalytically active histidine and two cationic residues (Gua) as potential anion-binding sites, show substrate hydrolysis in water. Metal-free catalysis with a rate enhancement of up to a factor of 175 over the uncatalyzed background reaction is observed.
Schmuck
Carsten
C
University of Würzburg, Institute of Organic Chemistry, Am Hubland, 97074 Würzburg, Germany. schmuck@chemie.uni-wuerzburg.de
Dudaczek
Jürgen
J
D002384:Catalysis; D020650:Combinatorial Chemistry Techniques; D004952:Esters; D010455:Peptides / Q000737:chemistry*; D014867:Water / Q000737:chemistry*
D004952:Esters; D010455:Peptides; D014867:Water