The surface chemistry of proteins makes them stable in complex biological environments. Scientists in the US have investigated why to enable peptide-based materials that resist non-specific interactions (stealth compounds) to be designed.
The cytoplasm is a crowded environment containing lots of different molecules but proteins resist non-specific interactions with these molecules. Understanding and mimicking nature’s resistance to non-specific interactions is key to addressing emerging challenges in chemistry, especially in practical applications where complex environments can degrade materials and surface coatings.
Here, the team has used structural bioinformatics to study proteins and molecular chaperones, which guide proteins from a misfolded or unfolded conformation back into a native conformation. They found that nature uses sequence design to modulate non-specific interactions so that the proteins function properly. Specifically, lysine and glutamic acid are the most abundant amino acids on the surface of proteins.
Link to journal article
Decoding nonspecific interactions from nature
A D White et al
Chem. Sci., DOI: 10.1039/c2sc21135a
