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andrew-wilson

Professor Andrew Wilson

The Wilson Group uses innovative synthetic methods to develop small molecule mimics and probes of biomacromolecule structure and function. A particular focus centers on the synthesis of non-natural amino acids (p-trifluoromethyldiazirine-phenylalanine and α-pentenyl-glycine). These reagents are used in cross-linking analysis of self-assembling peptides and to constrain peptides (so called “peptide-stapling”) for inhibition of protein-protein interactions. The group have developed and continue to develop a range of small molecules (accessible via solid-phase syntheses) to act as α-helix mimetics for inhibition of protein-protein interactions.

Wilson Group Website

Recent papers from the Wilson Group

1.
Preston GW, Radford SE, Ashcroft AE, Wilson AJ. 2014. Analysis of Amyloid Nanostructures Using Photo-cross-linking: In Situ Comparison of Three Widely Used Photo-cross-linkers. ACS Chem. Biol.. 9(3):761-768. http://dx.doi.org/10.1021/cb400731s
2.
Yeo DJ, Warriner SL, Wilson AJ. 2013. Monosubstituted alkenyl amino acids for peptide ?stapling?. Chem. Commun.. 49(80):9131. http://dx.doi.org/10.1039/c3cc45231j
3.
Azzarito V, Long K, Murphy NS, Wilson AJ. 2013. Inhibition of ?-helix-mediated protein?protein interactions using designed molecules. Nature Chem. 5(3):161-173. http://dx.doi.org/10.1038/nchem.1568

DISCIPLINES

  • Organic Synthetic Chemistry

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