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为了研究胰岛素受体结合部位的结构和功能，设计并用固相方法合成了３个六肽．在浓度大于１×１０３ｎｍｏｌ／Ｌ时，ｃｙｃｌｏ（Ｐｈｅ－Ｐｈｅ－Ｖａｌ－Ｌｅｕ－Ｔｙｒ－Ｇｌｙ）具有明显的胰岛素受体结合活力；Ｈ－Ｐｈｅ－Ｐｈｅ－Ｖａｌ－Ｌｅｕ－Ｔｙｒ－Ｇｌｙ－ＯＨ的这一活力则不明显；而Ｈ－Ｇｌｙ－Ｇｌｕ－Ａｒｇ－Ｇｌｙ－Ｐｈｅ－Ｐｈｅ－ＯＨ则增强胰岛素和其受体的亲和性．然而，它们都没有体内生物活性．这表明：环六肽部分模拟了胰岛素受体结合部位的空间构象；胰岛素受体结合部位的疏水性和其中的Ｂ２３Ｇｌｙ－Ｂ２４Ｐｈｅ－Ｂ２５Ｐｈｅ对胰岛素和其受体的结合起重要作用．
In order to study the structure and function of insulin receptor binding sites, three hexapeptides were designed and synthesized by solid phase method. The cyclo (Phe-Phe-Val-Leu-Tyr-Gly) had a significant insulin receptor binding activity at concentrations greater than 1 × 10 3 nmol / L; this was H-Phe-Phe-Val-Leu-Tyr-Gly-OH A vitality is not obvious; and H-Gly-Glu-Arg-Gly-Phe-Phe-OH enhance insulin and its receptor affinity. However, none of them have in vivo biological activity. This suggests that the cyclic hexapeptide partially mimics the spatial conformation of the insulin receptor binding site; the hydrophobicity of the insulin receptor binding site and the binding of B23Gly-B24Phe-B25Phe therein to insulin and its receptor play an important role.