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Antibiotic Selection

Antibiotic Selection

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Related Experiment Video

Updated: Jan 6, 2026

Standardized Modular Assembly of Polycistronic Operons with Modular Cloning (MoClo) using the In-Cloning toolkit

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Published on: September 2, 2025

Repurposing AGI-6780 to Activate ClpP and Target Gram-Positive Bacteria.

Roha Razzaq¹, Hazera Khatun Koly^1,2, Tahmina Hossain¹

¹Department of Biology and Microbiology, South Dakota State University, Brookings, South Dakota 57006, United States.

ACS Infectious Diseases

|November 10, 2025

Summary

This summary is machine-generated.

Researchers discovered a new antimicrobial strategy by targeting the bacterial ClpP protease. A novel compound, AGI-6780, effectively kills antibiotic-resistant bacteria by hyperactivating ClpP, offering a promising new therapeutic approach.

Keywords:

AGI-6780 ClpP antibiotic resistance antimicrobial agent protease

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Last Updated: Jan 6, 2026

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Published on: September 2, 2025

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Establishment of a High-throughput Setup for Screening Small Molecules That Modulate c-di-GMP Signaling in Pseudomonas aeruginosa

Establishment of a High-throughput Setup for Screening Small Molecules That Modulate c-di-GMP Signaling in Pseudomonas aeruginosa

Published on: June 30, 2016

Area of Science:

Microbiology
Drug Discovery
Biochemistry

Background:

The rise of antibiotic-resistant pathogens necessitates novel antimicrobial strategies.
Traditional antibiotics targeting essential bacterial processes are facing declining efficacy.
There is an urgent need for new antimicrobial agents with novel mechanisms of action.

Purpose of the Study:

To identify small molecules that hyperactivate the bacterial ClpP protease as a novel antimicrobial strategy.
To discover compounds that induce uncontrolled proteolysis leading to bacterial cell death.
To explore ClpP as an unconventional target for antimicrobial drug development.

Main Methods:

High-throughput in silico screening based on known ClpP-binding interactions.
Molecular docking simulations to predict binding affinity and prioritize compounds.
In vitro assays to evaluate antimicrobial activity and cytotoxicity.
Pharmacokinetic profiling of lead compounds.

Main Results:

AGI-6780 identified as a lead compound with high predicted affinity for the ClpP active site.
In vitro assays confirmed AGI-6780's efficacy against Gram-positive bacteria by targeting ClpP.
AGI-6780 demonstrated synergy with rifampicin and minimal cytotoxicity to human cell lines.

Conclusions:

AGI-6780 is a promising antimicrobial agent that uniquely targets the bacterial ClpP protease.
Exploiting ClpP offers a novel mechanism to combat antibiotic-resistant pathogens.
This approach represents a potential new avenue for developing effective antimicrobial therapies.