Khaing - It is not clear whether or not there occurs a direct binding of quercetin to heat shock proteins.

Possible factors influencing the binding include: potential binding to aromatic amino acid hydroxyl side chains, hydrophobicity of the peptide region, hindered conformation, hydrogen bonding, presence of double bonds in the heterocyclic C-ring, the number of aromatic –OH (hydroxyl) groups, etc. In the case of quercetin, this number is four (another hydroxyl group is located on the heterocyclic C-ring).

Potential binding to aromatic amino acid hydroxyl side chains (hydrogen bonds) might be reasonably anticipated. Quercetin molecule possesses dihedral angles (aromatic A-ring and the heterocyclic C-ring) which are planar (confer: Ramachandran torsional angles in peptides, and "The Ramachandran Map"). Points of interest include: O–H...O hydrogen bonds, and weak C–H...O; the molecular structure of quercetin in its solid state and the role of weak interactions (C–H...O, C–H… and π π, pi pi ) in assembling the molecules into an organized supramolecular structure .

If Hsp 70 were any guidance, quercetin could inhibit the induction of Hsp27 at the level of mRNA accumulation, and also at the level of post transcription.