Implications of aromatic–aromatic interactions: From protein structures to peptide models

摘要: With increasing structural information on proteins, the opportunity to understand physical forces governing protein folding is also expanding. One of significant non-covalent between side chains aromatic-aromatic interactions. Aromatic interactions have been widely exploited and thoroughly investigated in context folding, stability, molecular recognition, self-assembly processes. Through this review, we discuss contribution aromatic activity stability thermophilic, mesophilic, psychrophilic proteins. Being hydrophobic, amino acids tend reside hydrophobic interior or transmembrane segments In such positions, it can play a diverse role soluble membrane α-helix β-sheet stabilization. We highlight here some excellent investigations made using peptide models several approaches involving aryl-aryl interactions, as an increasingly popular strategy engineering. A recent survey described existence clusters (trimer, tetramer, pentamer, higher order assemblies), revealing self-associating property aryl groups, even folded structures. The application aromatics generation modern bionanomaterials discussed.