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Drug Development Targets in Ribosome

Drug Development in Ribosome

Research into bacterial ribosomes and the development of ribosome targeting antibiotics have been important in the fight against pathogenic bacteria, and have made outstanding contributions to human health. However, serious problems have developed, including bacterial drug resistance, and the toxicity of ribosomal antibiotics raised from their low selectivity. Great advances have been made to deal with the issues of drug resistance and selectivity/toxicity of ribosomes targeting antibacterial agents). Among all solutions, virtual screening and enzymatic activity assay-based screening to discover ribosome targeting antimicrobials with novel chemical structures or scaffolds are the most important strategies. However, the complexity of ribosome structures has impeded the development of receptor-based docking, molecular dynamics simulation, and activity-based screening. Recently, advances in ligand-based drug discovery and artificial intelligence have facilitated the virtual discovery of ribosomes targeting antimicrobials. In addition, with the development of cryo-electron microscopy technology and novel screening strategies, such as cell-free in vitro transcription/translation systems, opportunities to develop novel antimicrobials with more accuracy and efficiency are emerging. In this context, it is necessary to know more about the general targets of ribosome and ribosome inhibition-related targets.

Currently major concerns of ribosomes and ribosome-targeting antimicrobials.Fig. 1. Currently major concerns of ribosomes and ribosome-targeting antimicrobials. (Zhang, 2021)

Overview of Ribosome Targets

Ribosomes are critical organelles for the survival and growth of bacteria, which act as bridges between genetic information and proteins. They are composed of three rRNA chains (16S, 23S, and 5S) containing major functional sites and approximately 54 protein molecules. The 16S rRNA and more than 20 proteins form the 30S small subunit; the 5S rRNA, 23SrRNA, and more than 30 proteins form the 50S large subunit; and the combination of the two subunits forms the ribosomal 70S complex. In a protein synthesis process, the transfer RNAs (tRNAs) read codons of the messenger RNA (mRNA) and deliver specific amino acids to the A and P sites of the ribosome. Meanwhile, a series of cofactors, including GTP, initiation factors, elongation factors, release factors, and recycling factors, interact with the 70S complex, which moves on mRNA and operates in a continuous cycle thereby completing the translation of genetic information. Using the gene-editing method, researchers found that overexpression of rRNA fragments simulating the h34 of 16S rRNA, which is the binding region of the ribosomal antibiotic spectinomycin, results in bacterial resistance to spectinomycin. Similarly, previous reports confirmed that the addition of excessive EF Tu can restore the in vitro translation process of ribosomes in the presence of the EF Tu inhibitors such as amythiamycin.

The translation process of bacterial ribosomes and ribosome targeting antibiotics acting on different stages.Fig. 2. The translation process of bacterial ribosomes and ribosome targeting antibiotics acting on different stages. (Zhang, 2021)

Services at Creative Biolabs

To date, about 60% of approved antibacterial agents work by targeting ribosomes. The importance of ribosomes in drug development is self-evident. With years of experience focusing on ribosome studies, Creative Biolabs has established a comprehensive technology platform for ribosome-related services. The platform is equipped with advanced technology, up-to-date facilities, and experienced experts. Thus our platform is capable of providing customer-satisfied services including but not limited to:

If you are also focusing on ribosome studies or you have met any problems during your research, please feel free to contact us for more information.


  1. Zhang, L.; et al. Ribosome-targeting antibacterial agents: Advances, challenges, and opportunities. Med Res Rev. 2021, 41(4): 1855-1889.
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