AI Article Synopsis
- Researchers developed an oligoamide foldamer that can selectively recognize and bind to specific protein surfaces, particularly targeting DM2.
- This recognition inhibits the interaction between DM2 and the p53 protein, which is crucial for cancer biology.
- The effectiveness and selectivity of this inhibition depend on the arrangement and orientation of functional groups on the foldamer, making stereochemistry pivotal in targeting other proteins like Mcl-1 and NOXA-B.
Article Abstract
The development of foldamers capable of selective molecular recognition of solvent exposed protein surfaces represents an outstanding challenge in supramolecular chemical biology. Here we introduce an oligoamide foldamer with well-defined conformation that bears all the hallmarks of an information rich oligomer. Specifically, the foldamer recognizes its target protein DM2 leading to inhibition of its protein-protein interaction with p53 in a manner that depends upon the composition, spatial projection and stereochemistry of functional groups appended to the scaffold. Most significantly, selective inhibition of p53/DM2 can be achieved against four other targets and the selectivity for p53/DM2 inhibition Mcl-1/NOXA-B inhibition is critically dependent upon the stereochemistry of the helix mimetic.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5646261 | PMC |
| http://dx.doi.org/10.1039/c4sc03559c | DOI Listing |
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