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

Area of Science:

• Biochemistry
• Structural Biology
• Biophysics

Background:

• Protein folding is governed by various physical forces, including non-covalent interactions between amino acid side chains.
• Aromatic-aromatic interactions are significant non-covalent forces crucial for protein structure, function, and assembly.

Purpose of the Study:

• To review the role of aromatic interactions in the stability and activity of proteins from thermophilic, mesophilic, and psychrophilic organisms.
• To explore the application of aryl-aryl interactions in protein and peptide engineering.
• To discuss the self-assembly of aromatic groups and their use in bionanomaterials.

Main Methods:

• Literature review of studies on protein structure and function.
• Analysis of investigations using peptide models and aryl-aryl interaction strategies.
• Survey of aromatic cluster formation in folded proteins.

Main Results:

• Aromatic interactions contribute to protein stability and activity across a wide range of temperatures.
• Hydrophobic aromatic amino acids are often found in protein interiors or transmembrane segments, stabilizing secondary structures like alpha-helices and beta-sheets.
• Aromatic groups exhibit self-associating properties, forming clusters and enabling applications in protein and peptide engineering and bionanomaterials.

Conclusions:

• Aromatic-aromatic interactions are fundamental to protein structure, stability, and function.
• The understanding and manipulation of these interactions offer promising avenues for protein engineering and the development of novel bionanomaterials.