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Cobb Research Group

Foldamer Research

Our interest in foldamers originated from our work in methodology where we devised asymmetric syntheses towards unnatural amino acids. Like the normal amino acids that appear in nature, these can fold into higher order structures when incorporated into certain oligomeric sequences. This folding will organise the placement of functionality, leading to applications in - for example -catalysis, molecular recognition and peptidomimetics.

Our efforts in this area are largely centred around heteromeric sequences of 𝜶- and 𝛾- or 𝜹-amino acids. Depending upon the nature of these unnatural amino acids, we can access unusual secondary structures where the arrangement of functionality has not been see before and so can provide us with unique opportunities in the above applications. 

3D molecular structure of a protein segment with highlighted bonds.

Asymmetric Methodology

Our groups origins are in the development of asymmetric methodology. We have developed routes to complex, densely functionalised molecules ranging from alkaloids and unnatural nucleic acids to terpenes and homologated amino acids, which we apply to our foldamer work. We are particularly interested in organocatalytic approaches and are using these principles and approaches in the design of our catalytic helices.

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