Description:

INV-21034

 

Background 

Due to the rapid development of antibiotic resistance in bacteria, there is a need for the identification of new antibiotic target sites. Translation of RNA's in proteins is one of the key steps for the survival of bacteria which is completed at the ribosome. The bacterial ribosome is a massive ribonucleoprotein assemble. It undergoes large scale rearrangements to translate messenger RNA into proteins. There are conformations of assembled 50S and 30S ribosomes that are responsible for accurate translation. Here, researchers have put forward hybrid conformations of the ribosome as novel antibiotic targets to combat antibacterial resistance.

 

Technology Overview 

Researchers at Northeastern University have developed theoretical models, called structure-based models, to simulate specific substeps of the elongation process in the ribosome. All possible conformations of the ribosomes were studied to find the target conformation that would be transient but critical to the dynamics of translation. P/P and P/E conformations are essential for protein synthesis, the studies show that a small region of the ribosome appears to limit the rate. These regions (around Asn29 of protein L33) are unique to bacteria, and are conserved across bacteria. Therefore, binding a small molecule to this point could stop protein synthesis in bacteria with minimal side effects.

 

Benefits

  • Identification of novel target
  • Based on the known target, small molecules can be designed
  • Completely computational design
  • Time and cost-effective method

Applications

  • Broad-spectrum antibiotics

 

Opportunity

  • License
  • Partnering
  • Research collaboration

 

 

 

 

 

Patent Information:
For Information, Contact:
Mark Saulich
Associate Director of Commercialization
Northeastern University
m.saulich@northeastern.edu
Inventors:
Paul Whitford
Mariana Levi
Keywords:
antibiotic resistance