In a world-first, researchers from The University of Queensland and University of Washington (UW) have produced tailor-made peptides – an advance expected to help improve drug design and environmentally-friendly pesticides.
Peptides – naturally occurring chains of amino acids – are highly desired in drug development but can be unstable.
The team from the UQ's Institute for Molecular Bioscience (IMB) and UW's Institute for Protein Design has designed ultra-stable peptide scaffolds that can be used in a range of biotechnological applications.
Professor David Craik said these peptides could have excellent pharmaceutical properties, combining the stability and tissue penetration of small-molecule drugs with the specificity of much larger protein therapeutics.
"Peptides are generally more specific than traditional 'small molecule' drugs, which means they have fewer side effects and are more potent," Professor Craik said.
"Until now, researchers have had to rely on natural peptides to provide drug scaffolds, which meant their work was limited by the availability of natural peptides with a particular shape and chemical characteristics.
"Along with Professor David Baker's team from UW, we have developed a new method where we can tailor the peptides into virtually any shape, and encourage them to adopt useful chemical characteristics and resist biological degradation.
"This is a major step forward that opens new avenues in peptide research and is expected to have a significant global impact."
The research was published in Nature.
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Gaurav Bhardwaj et al. Accurate de novo design of hyperstable constrained peptides, Nature (2016). DOI: 10.1038/nature19791