Helix Mimetics
The alpha-helix is the most common repeating structure found in proteins. Some proteins consist almost entirely of helical segments folded back on themselves - as can be seen in the image to the left. The red spiral is a helical peptide (Bim) bound to a small protein containing seven helical segments (Bcl-xL - blue). You can examine the structure in 3D here.
Why make a helix mimetic?
Nature has a limited set of structural and chemical elements. The alpha-helix is an important and central part of protein structure and hence inevitably helical domains are involved in many significant biological processes. To modulate those processes we may need to use a helical peptide or something that imitates the shape of a helix.
Short helical peptides are not very stable - they tend to unravel and are readily destroyed by natural proteases, hence they are difficult to use as drugs. These issues led to the idea of stabilising helical peptides by chemical modification - or otherwise reproducing the function of the helix with a "mimetic" - a more stable molecule that acts in the same way as the natural helix.
These ideas have been around for many years - but developing good technology has proven difficult. Oroborus scientists have recently developed new technology for stabilising peptide helices. This technology has demonstrated strong stabilisation of short peptides and has the potential to be best-in-class due to technical advantages over other approaches.
Some further information about helix mimetic technology and targets can be found on our other website www.peplix.com
