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Updated: Jan 10, 2026

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

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Published on: October 26, 2015

Development of Cell-Permeable Adenylosuccinate Lyase Inhibitor.

Yijia Hu^1,2, Young-Sam Lee^1,3

¹Department of Biology, Johns Hopkins University, Baltimore, MD 21218, USA.

Methods and Protocols

|November 24, 2025

Summary

This summary is machine-generated.

Researchers developed a cell-permeable inhibitor for adenylosuccinate lyase (ADSL), an enzyme linked to cancer and neurodevelopment. This new compound shows promise for studying ADSL

Keywords:

adenylosuccinate lyase inhibitor nucleotide screening

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Area of Science:

Biochemistry
Enzyme Inhibition
Drug Discovery

Background:

Abnormal adenylosuccinate lyase (ADSL) activity is implicated in cancer and neurodevelopmental disorders.
A significant limitation in studying ADSL's role is the lack of cell-permeable inhibitors.

Purpose of the Study:

To develop a cell-permeable inhibitor of ADSL.
To identify and synthesize fragments of a previously identified lead compound (NF-449) with improved cell permeability.

Main Methods:

High-throughput screening to identify lead compounds.
Chemical synthesis of NF-449 fragments.
Enzyme inhibition assays using purified human ADSL.
Cell-based assays to determine IC50 values in HeLa cells.

Main Results:

A synthesized fragment, 2,2'-(1,3-phenylenebis(carbonylimino))-bisbenzenesulfonate, was identified as a competitive inhibitor of purified human ADSL (Ki = 0.4 µM).
The triethylammonium salt of this fragment demonstrated ADSL inhibition in HeLa cells with an IC50 of 0.4 µM.
The compound exhibits improved cell permeability compared to the original lead compound.

Conclusions:

A novel, cell-permeable ADSL inhibitor has been developed.
This compound is a valuable tool for in vitro studies of ADSL.
Further optimization may yield reagents suitable for in vivo research.