The work aims to method of improving improve the hydrophobicity of metal surface after reaction was studied by adjusting the peptide chain structure of peptides reacting with metal. It took the same peptide of tTwo different structures of the same peptide were adopted: L-type and D-type antitone reacting reacted respectively with stainless steel and, the change of metal material’s hydrophobicity was determined through CA. FTIR showed the existence of organic peptide on the surface of the material. Hydrophobic group dodecanoic acid was added to L-type peptide and D-type peptide respectively to obtain two new peptides with different structures: L’-type peptide and D’-type antitone peptide. Two peptides respectively reacted with the stainless steel. FTIR and CA were used to study the connection of hydrophobic groups and the effect on the hydrophobicity of materials. After the action, the surface contact angle of the stainless steel surface modified by the D-type antitone peptide was higher than that of the stainless steel surface modified by the L-type peptide, which was changed from 39.7 degree to 80.1 degree. After the insertion of the hydrophobic group, the solubility of the peptide in the PBS decreased. By the initial solution in the organic solvent, the peptide dissolved completely in the PBS. After the action of the D’-type peptide solution with the metal material, the surface had a higher surface contact angle than that of L‘-type peptide, which was 89.4 degree and 87.4 degree respectively. The effect of former was better. By adjusting the structure of the peptide chain of biopeptide, the hydrophobic properties of the modified metal surface can be changed, thus providing a powerful data support for preparing a metal materials with good hydrophobic properties by adjusting the peptide chain structure and the hydrophobic group of the metal reaction peptide.