In order to explore the interaction between peanut protein (PP) and polyphenols， this paper first used molecular docking technology to select active components with strong binding effect from 100 polyphenols. The mechanism of interaction between peanut protein (PP) and polyphenols was investigated by multispectral method and scanning electron microscopy. Molecular bonding results showed that silymarin (Sil)， epigallocatechin gallate (EGCG)， rosmarinic acid (RA) and luteolin (Lut) had higher binding scores to peanut protein. The value of kq was greater than 2.0×1010 L/(mol·s)， indicating that the interaction between the four polyphenols and peanut protein was mainly static quenching. The binding constants Ka of Sil， EGCG， RA， Lut and PP were 7.63×105， 2.91×107， 2.19×106 and 6.52×104 L/mol， respectively. It is proved that the combination ability of EGCG and PP is better. The main interaction forces of epigallocatechin gallate， silymarin and rosmarinic acid with peanut protein were hydrogen bond and van der Waals force. The interaction between luteolin and peanut protein was mainly hydrophobic. The number of binding sites is 1； After RA， Lut and PP， the β-corner content increased by 30.74% and 17.05%， respectively， and the β-fold content of Lut increased by 8.04%， and the α-helix changed to β-corner and β-fold. RA is irregularly curled into a β-angle transition. In summary， EGCG and PP showed the strongest binding ability， and RA caused greater structural changes in PP， which could provide reference data for the development and utilization of peanut protein.