Publications by authors named "Neil Rankine"
Directed screening has identified a novel series of MMP13 inhibitors that possess good levels of activity whilst possessing excellent selectivity over related MMPs. The binding mode of the series has been solved by co-crystallisation and demonstrates an interesting mode of inhibition without interaction with the catalytic zinc atom.
View Article and Find Full Text PDFA number of molecular recognition features have been exploited in structure-based design of selective Cathepsin inhibitors.
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- The text presents a new method for inhibiting the alphavbeta3 integrin, which is a protein that plays a role in various biological processes.
- This approach focuses on using specially designed compounds that achieve nanomolar (nM) potency, meaning they are very effective at low concentrations.
- Importantly, this method does not rely on the traditional arginine binding site for its effectiveness, suggesting a novel mechanism of action.
A series of potent Cathepsin L inhibitors with good selectivity with respect to other cysteine Cathepsins is described and SAR is discussed with reference to the crystal structure of a protein-ligand complex.
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