SINGAPORE - A new class of ultrasmall peptides developed by the Institute of Bioengineering and Nanotechnology (IBN) may offer scientists a window into understanding the formation mechanism of abnormal proteins in degenerative diseases.
This may help researchers combat diseases such as Alzheimer's, diabetes and cancer by allowing them to design appropriate drugs to inhibit and control the formation of such proteins.
Amyloids, or fibrous aggregates of abnormally folded proteins, are a common feature in degenerative diseases. Amyloids occur naturally in the body, but despite decades of research, their mechanism of formation remains unknown, hampering drug development efforts.
Building on earlier research, the team found a striking similarity between the structure of synthetic peptides developed by IBN in 2011 and the protein structure of naturally occurring amyloids.
IBN Team Leader and Principal Research Scientist Dr Charlotte Hauser elaborated: "This is the first proof-of-concept that our peptides self-assemble in the same way as naturally occurring amyloid sequences.
"Knowing that the process of amyloid formation is common across various chronic degenerative diseases, our goal is to identify the specific trigger so that we can design the appropriate drugs to inhibit and control the aggregate formation."
In addition, this study supports the growing evidence that early intermediates are more toxic than the final amyloid fibers, and may even be the driving force behind amyloid formation.
Patent applications have been filed on this research, and the next step of this project is pre-clinical evaluation of ultrasmall peptide therapeutics. IBN will also investigate other amyloid disorders such as corneal dystrophy, which can result in blindness.