Proteins are like a body’s in-house Lego set. Most of the time, these large, complex molecules fold correctly—but sometimes they misfold, which can lead to a number of different diseases including ALS, Alzheimer’s and Parkinson’s. Many of these interactions, both folded and misfolded, are affected by the surface chemistry of proteins. Specifically, how sticky the proteins are.
The problem is that researchers don’t have highly sensitive tools or methods to measure the stickiness, or the hydrophobicity, of protein surfaces. Now, an interdisciplinary team at Michigan Technological University has gathered new tools to solve the case of the sticky protein. Their work on improving the sensitivity of hydrophobicity detection just came out in Scientific Reports.
Ashutosh Tiwari, an associate professor of chemistry at Michigan Tech and corresponding author on the study, compares a sticky protein to a ball covered in glue with a few craft pom-poms stuck to it.
“When you roll it on the ground, it will non-specifically bind with a lot of gunk,” Tiwari says. “What we want to know is how much of that surface is sticky, and if we can define it in terms of stickiness, then we will know the protein’s tendency to bind with gunk, which reflects its ability to interact with other proteins.”
Many of those interactions are a normal function of proteins, but biochemists think extra stickiness can drive the protein misfolding and aggregation process. Protein aggregates are called many names including amyloid, plaques, tangles, inclusions, and pick bodies—the body’s signatures for many neurodegenerative diseases.
For the full story, video and photos, see http://www.mtu.edu/news/stories/2015/december/case-sticky-protein-interdisciplinary-team-puts-together-clues-better-sense-surface-hydrophobicity.html
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