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Updated: Jan 28, 2026

Detection of Protein S-Acylation using Acyl-Resin Assisted Capture
Published on: April 10, 2020
The studies on chemoselective promiscuous activity of hydrolases on acylals transformations
Dominik Koszelewski1, Ryszard Ostaszewski1
1Institute of Organic Chemistry, Polish Academy of Sciences, Kasprzaka 44/52, 01-224 Warsaw, Poland.
Abstract:
Chemoselective, mild and convenient protocol for the hydrolysis of the synthetically relevant acylals via promiscuous enzyme-catalyzed hydrolysis has been developed. It has been shown that promiscuous activity of the used hydrolases dominates their native activity related with carboxylic esters hydrolysis. The main advantage of the present methodology is that it can be conducted under neutral conditions at room temperature. Moreover, complete deprotection of acylals takes place within 10-20 min. Developed protocol can be used with compounds having a variety of hydrolytic labile groups since the cleavage is proceeded under neutral conditions and occurs exclusively on acylal moiety. Further this protocol was extended by the tandem Passerini multicomponent reaction leading to the α-acetoxy amides using acylals as the surrogates of the carbonyl components to P-MCR.
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