A protein's stickiness is a result of surface hydrophobic interactions that are important for many biological functions. An interdisciplinary team at Michigan Technological University has assembled new tools to solve the case of the sticky protein. Their work on improving hydrophobicity detection was published in Scientific Reports on December 18, 2015.
Using the fluorescent probes, the team measured hydrophobicity in three proteins: Bovine Serum Albumin (BSA), apomyoglobin and myoglobin. Compared to a commonly used commercial sensor (ANS), these new BODIPY-based hydrophobic sensors showed much stronger signal strengths, with up to a 60-fold increase in BSA.
Proteins are like a body's in-house Lego set. These large, complex molecules are made up of building blocks called amino acids. Most of the time, proteins fold correctly, but sometimes they can misfold. This misfolding causes the proteins to get sticky, and that can promote clumping, or aggregation, which is the hallmark of several neurodegenerative diseases such as ALS, Alzheimer's and Parkinson's.