The interaction between homocatechol and bovine serum albumin(BSA) was studied. The results showed that homocatechol could quench the fluorescence of BSA. A macromolecular complex with weak fluorescence was spontaneously formed with BSA mainly through hydrophobic bond， and at least one binding site of homocatechol on BSA at 298， 310 K and 320 K. The binding constants of homocatechol to BSA were 5.908×102， 5.424×104， 1.535×106 L/mol. It is speculated that the quenching of BSA by homocatechol was mainly dynamic quenching， and there is also a static quenching process. The cold field emission scanning electron microscopy showed that 2 μmol/L homocatechol could promote the dissolution of protein and made its distribution more uniform. When the concentration of homocatechol was 2 μmol/L， the protein would aggregate. Molecular docking analysis showed that homocatechol was stably bound to the hydrophobic pocket of BSA Subdomain IIA (site I) mainly through hydrophobic bond， hydrogen bond and van der Waals force.