ArticleChemistry (Weinheim an der Bergstrasse, Germany)2025
Water-Soluble Peptoids with Two Different Binding Sites for Strong ATP Chelation.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Adenosine Triphosphate (ATP) is the activator of many enzymes, including kinases, that play a significant role in various medical conditions such as cancer. Therefore, inhibiting ATP-dependent enzymes requires to disable its binding to enzymes, and this can be done by developing potent ATP chelators. Currently, there are two main types of chelators: one that binds ATP via zinc complexes of nitrogen-based ligands, such as 2,2';6',2″-terpyridine (Terpy), which target the phosphate ligands, and another one containing phenylboronic acid (PBA) to bind the diols within the ribose. Herein, we report on a unique chelation approach that combines these two binding strategies in one scaffold; we use peptidomimetic oligomers called peptoids that incorporate both Zn(Terpy) and PBA as strong, water-soluble ATP binding inhibitors. These peptoids demonstrated high affinity to ATP, where the highest is K
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