Explore Phenol, 1-Naphthol and 2-Naphthol Sidechains
Aromatic amino acids are involved in critical interactions at protein-protein interfaces, and in protein-carbohydrate and protein-oligonucleotide complexes. Additionally, Tyr analogs have tunable acidity and redox potential, and can be handles for bioorthogonal conjugation.
Expanding the aromatic repertoire to include phenol and naphthol sidechains allows for fine tuning of binding site interactions by exploiting hydrophobic interactions, π-stacking, and hydrogen and halogen bonding.
Incorporate tyrosine analogs into your workflow to:
- improve binding affinity & specificity
- create π–π or cation–π interactions
- increase protease resistance
- prevent oxidation
- improve membrane permeability
- synthesize analogs of dopamine
