Abstract

We communicate the results of calculations and selection methods, and identify the properties, of inhibitors that block the formation of high-molecular-weight structures from amyloid peptides, with their blocking mechanism explained. We consider in detail the biochemical requirements for, and the criteria and conditions for identification of, inhibitors that prevent amyloids from forming higher-order structures. For the inhibitors, we investigate modified peptides that, by combining with amyloid peptides, will form stable dimers thereby preventing amyloids from participating in ever different and new biochemical reactions. We address biochemical reactions of the amyloids with amyloid peptides of a similar kind, but their possible interaction with blood vessel walls is beyond the scope of this work. For the criterion of dimer complex stability, we use (i) logarithm of the condition number of potential energy matrix of paired electrostatic interaction between amino acid residues and (ii) the differential entropy of a multidimensional normal distribution.

中文翻译：

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二聚体复合物之间的静电相互作用分析。第二部分：APP蛋白衍生物抑制剂的标准和条件

摘要

我们交流了计算和选择方法的结果，并确定了可阻止淀粉样蛋白肽形成高分子量结构的抑制剂的性质，并说明了其阻断机理。我们详细考虑了防止淀粉样蛋白形成高级结构的抑制剂的生化要求以及鉴定的标准和条件。对于抑制剂，我们研究了修饰的肽，该修饰的肽与淀粉样蛋白肽结合将形成稳定的二聚体，从而防止淀粉样蛋白参与千差万别的生化反应。我们讨论了淀粉样蛋白与相似类型的淀粉样蛋白肽的生化反应，但它们与血管壁的可能相互作用不在本研究范围之内。对于二聚体稳定性的标准，