Docking Evaluation of the Interaction Between Green Tea Active Ingredient, l-Theanine and Human Serum Albumin

Interaction of one of the green tea active ingredients, l-theanine with the major transport protein of human blood circulation, human serum albumin (HSA) was investigated using molecular docking analysis. Site-specific docking simulation suggested binding preference of l-theanine to Site 1 of HSA. The binding site is proposed to be a cleft surrounded by both polar and nonpolar residues. l-Theanine binds to the protein through hydrophobic interactions as well as hydrogen bonds formed between Lys residues (195 and 199) of HSA and l-theanine.