A team from the University of Bath has created peptides that can permanently inhibit the cJun protein, which plays a role in cancer development. This strategy employs a novel screening technique to discover irreversible inhibitors, marking the first time such an approach has been used in this area. The findings have been published in Advanced Science could transform the approach to treating specific types of cancer.
Transcription factors such as cJun play a crucial role in regulating gene expression and are frequently found to be abnormal in cancerous conditions. In contrast to small molecules, peptides have the capability to target these proteins with greater precision. The TBS approach enables the direct assessment of their efficacy within cellular environments, thereby discarding potential toxins or non-functional options.
The inhibitor peptide created by scientists attaches permanently to cJun, stopping it from interacting with DNA. Unlike a molecular harpoon, this method offers irreversible protein blockage. Tests conducted in the lab verified its ability to penetrate cells as well as its selective nature.
The TBS platform marks significant progress in drug screening. It assesses peptide activity within an authentic cell setting, encompassing enzymes like proteases along with various disruptive proteins. This methodology has potential applications beyond just currently ‘undruggable’ targets.
The next phase will focus on verifying the efficacy of these inhibitors using preclinical cancer models. The team anticipates that their technology could facilitate the identification of novel drug candidates targeting areas previously deemed unreachable.
This project received support from the Medical Research Council and the The Biotechnology and Biological Sciences Research Council It signifies a crucial step in combating cancers associated with the disruption of transcription factors.
What is the mechanism of action for peptide inhibitors?
Peptide inhibitors are crafted to selectively attach to specific proteins such as cJun and inhibit their function. In contrast to small molecules, these peptides can emulate natural protein-protein interactions, providing higher precision.
For cJun, the inhibitor peptide attaches permanently, which stops the protein from pairing up and attaching to DNA. This mechanism is essential for halting the growth of cancer cells.
Adjusting the peptide for permanent attachment marks a significant advancement. This guarantees that the inhibition continues unabated within the ever-changing cellular milieu where proteins are continually being produced and broken down.
This method could be modified to address additional transcription factors linked to different illnesses, providing novel routes for therapy.
Source: Advanced Science
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