Craig Hutton is from the University of Melbourne, in Australia, and he investigates a solid-phase method to synthesize cross-linked peptides, to enable the team to study the peptides role in Alzheimer's disease.

What inspired you to become a scientist?
My father is an electronic engineer, so as a child our shed was always full of interesting gadgets - magnets, motors, multimeters and the like - with which to experiment. This curiosity progressed to me and my brothers, where we started experimenting with household chemicals - occasionally with frightful combinations! I often wonder how none of us were injured, or how the shed wasn't burnt down.
At the University of Adelaide I undertook an undergraduate research project with Professor Chris Easton and enjoyed it so much I continued in the Easton group to pursue my PhD. To this day, Chris remains an inspiring mentor and great friend.

What was your motivation behind the work described in your ChemComm article?

My research group had been working in the area of cross-linked amino acids for a few years when Kevin Barnham from the Department of Pathology, University Of Melbourne, approached me regarding a collaboration. The project involves preparing cross-linked amyloid-beta peptides in order to study their role in Alzheimer's disease. We needed a method applicable to the synthesis of side-chain cross-linked peptide dimers (rather than N- or C-terminal linked dimers), and investigated the solid-phase method described in this article. We have applied the method to the synthesis of alkyl-linked amyloid peptides, and anticipate that the method will be applicable to a variety of cross-linked peptide dimers.

Why did you choose ChemComm to publish your work?

ChemComm has a broad readership and is one of the most highly regarded international chemistry journals.

Where do you see your research heading next? 

We are currently applying our methodology to the preparation of physiologically relevant dityrosine-linked amyloid-beta peptides. We hope to prepare the dityrosine-linked (1-40) and (1-42) amyloid-beta dimers to determine whether such species are neurotoxic and play a role in the progression of Alzheimer's disease.

What do enjoy doing in your spare time? 

I play baseball to keep active, and any remaining spare time is filled with kicking a football in the back yard with my three young children.

If you could not be a scientist, but could be anything else, what would you be?
An orthopaedic surgeon. Having been through orthopaedic surgery myself, and witnessing my son's operation, I am in awe of the life-saving and life-changing outcomes that highly skilled surgeons can achieve. Alternatively a professional baseball player!

Interviewed by Kathryn Sear