目的 通过调整与金属反应的肽的肽链结构，提高反应后金属表面的疏水性。方法 取同种肽两种不同结构（L-型和D-型反序结构）分别与金属不锈钢作用，通过CA测定材料疏水性的变化，采用FTIR显示有机肽在材料表面的附着情况。分别在L-型和D-型肽上接入疏水基团十二烷酸，获得两种新的不同结构的肽：L?-型肽和D?-型肽。两种肽分别与金属不锈钢作用，利用FTIR 和CA研究疏水基团的接入及其对材料疏水性的影响情况。结果 与金属不锈钢作用之后，D型肽反序结构修饰的不锈钢表面接触角比L型肽修饰有所提高，由原来的39.7?变成80.1?。接入疏水基团后的肽在PBS中的溶解度减小，用有机溶剂初溶之后再溶入PBS中，生物肽全部溶解。该肽溶液与金属材料作用之后，D?型肽比L?型肽作用的表面接触角更高，分别为89.4?和87.4?，前者作用效果更好。结论 通过调整生物肽肽链的结构，可以改变改性金属材料表面的疏水特性，为进一步通过调整金属反应肽的肽链结构和疏水基团的种类得到具有良好疏水性能的金属材料提供了有力的数据支撑。

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.