Related Experiment Video
Updated: Mar 27, 2026

Analyzing DNA-Protein Interactions with Streptavidin-Based Biolayer Interferometry
Published on: January 17, 2025
Identification and Optimization of Anthranilic Acid Based Inhibitors of Replication Protein A
James D Patrone1,2, Nicholas F Pelz1, Brittney S Bates1
1Department of Biochemistry, Vanderbilt University, Nashville, TN, 37232, USA.
Abstract:
Replication protein A (RPA) is an essential single-stranded DNA (ssDNA)-binding protein that initiates the DNA damage response pathway through protein-protein interactions (PPIs) mediated by its 70N domain. The identification and use of chemical probes that can specifically disrupt these interactions is important for validating RPA as a cancer target. A high-throughput screen (HTS) to identify new chemical entities was conducted, and 90 hit compounds were identified. From these initial hits, an anthranilic acid based series was optimized by using a structure-guided iterative medicinal chemistry approach to yield a cell-penetrant compound that binds to RPA70N with an affinity of 812 nm. This compound, 2-(3- (N-(3,4-dichlorophenyl)sulfamoyl)-4-methylbenzamido)benzoic acid (20 c), is capable of inhibiting PPIs mediated by this domain.
More Related Videos
08:33Nucleocapsid Annealing-Mediated Electrophoresis NAME Assay Allows the Rapid Identification of HIV-1 Nucleocapsid Inhibitors
Published on: January 19, 2015
10:24A Fluorescence-based Protocol for Preliminary Screening of Protein Synthesis Inhibitors from Natural Sources
Published on: January 27, 2026
Related Concept Videos
Inhibitors of Viral Protein Synthesis
Inhibitors of Bacterial Protein Synthesis
Inhibitors of Bacterial DNA Synthesis