Open AccessSelective Hydrolysis of Aryl Esters under Acidic and Neutral Conditions by a Synthetic Aspartic Protease Mimic
Author(s) -
Ishani Bose,
Yan Zhao
Publication year - 2021
Publication title -
acs catalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.898
H-Index - 198
ISSN - 2155-5435
DOI - 10.1021/acscatal.1c00371
Subject(s) - chemistry , hydrolysis , catalysis , aryl , nucleophile , hydroxide , leaving group , organic chemistry , substrate (aquarium) , protease , active site , enzyme , combinatorial chemistry , proteases , alkyl , oceanography , geology
Aspartic proteases use a pair of carboxylic acids to activate water molecules for nucleophilic attack. Here we report a nanoparticle catalyst with a similar catalytic motif capable of generating a hydroxide ion in its active site even under acidic reaction conditions. The synthetic enzyme accelerated the hydrolysis of para -nitrophenyl acetate (PNPA) by 91,000 times and could also hydrolyze nonactivated aryl esters at pH 7. The distance between the two acids and, in particular, the flexibility of the catalytic groups in the active site controlled the catalytic efficiency. The synthetic enzyme readily detected the addition of a single methyl on the acyl group of the substrate, as well as the substitution pattern on the phenyl ring.