中文摘要：

为了促使多肽亲和配基在实际分离研究中得到广泛应用，利用Fmoc固相合成法对从噬菌体展示肽库中筛选得到的与胰岛素具有高特异性亲和的七肽片段（HWWWPAS）进行了合成．在合成中发现，肽段序列中脯氨酸的存在会严重影响合成结果．去除脯氨酸后，目标产物的收率从0％提高到11．6％；同时，七肽序列中丙氨酸的存在也会影响合成效果．若将丙氨酸除去，合成收率会明显提高（达到76％），特别是将丙氨酸更换为谷氨酸产物的收率和纯度均可达到70％以上．利用固定化六肽片段（HWWWES）进行亲和吸附实验的结果表明，改造后的六肽配基与原先的七肽配基具有相似的亲和吸附效果．

英文摘要：

A heptapeptide （HWWWPAS） with high affinity for insulin is screened from phage peptide library and then synthesized by Fmoc solid-phase synthesis method. The result shows that Pro has unfavorable effect on synthesis of heptapeptide and the product yield can be increased from 0% to 11.6% by deleting Pro. In the meanwhile, Ala in the heptapeptide can also affect peptide synthesis. The deletion of Ala can gain a yield of 76%. Especially a Glu substitute for Ala has significant enhancement in both product yield and purity （over 70%）. Affinity chromatography is carried out using reconstructive hexapeptide （HWWWES） as affinity ligand. And the result proves that the modified hexapeptide has the same behavior as the original one （HWWWPAS）.