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以最小二乘叠合技术和图象显示技术对DPI、二锌胰岛素及其他一些衍生物结构进行了深入的比较和分析,确认与受体分子的结合相互作用是发生在胰岛素分子的一个两性表面上,其中部是由许多疏水残基构成的面积约150~2的疏水表面,而一些极性基团在其周围构成亲水带区。疏水表面通常被运动性很大的B链羧端肽段所覆盖,不受极性溶剂分子的干扰。两性表面在方位上与分子在二体中的缔合面构成约20°的夹角。Al-L-Trp胰岛素及Al-D-Trp胰岛素结构详细的比较结果,既很好地解释了两者在生物活性上的显著差异,又进一步确认了我们所提出的胰岛素分子与其受体结合的作用模型。
In-depth comparison and analysis of the structures of DPI, di-zinc insulin and some other derivatives by the least-squares superposition technique and image display technology confirm that the binding interaction with the receptor molecule occurs on an amphiphilic surface of the insulin molecule , The middle part of which is a hydrophobic surface consisting of many hydrophobic residues with an area of about 150-2, while some polar groups form a hydrophilic band around it. Hydrophobic surfaces are usually covered by highly motile B-chain carboxy-terminal peptides that are not interfered with by polar solvent molecules. The amphoteric surface forms an angle of about 20 ° in azimuth with the associated surface of the molecule in the body. The detailed comparison of Al-L-Trp insulin and Al-D-Trp insulin structures not only explains the significant difference in biological activity between the two, but also further confirms that our proposed insulin molecule binds to its receptor Role model.