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Analysis of Electrostatic Interaction between Dimer Complexes. Part I: A Method for Selecting Inhibitors of APP Protein Derivatives


We present an unconventional method that provides qualitative evaluation of the ability of amyloid peptides to form high-molecular-weight structures and enables us to resolve the stability issue of amyloid dimer complex by means of introduced quantitative descriptors, which are (i) the logarithm of the condition number of matrix of potential energy of paired electrostatic interaction between amino acid residues and (ii) the differential entropy for a multidimensional normal distribution, which enables us to predict the formation of higher-order structures such as oligomers, protofibrils, and fibrils, as the stability state is reached. Therefore, the main strategy for preventing amyloid formation upon their aggregation into high-molecular-weight structures is to ensure their stabilization at the level of dimer complexes.

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Correspondence to T. V. Koshlan.

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Translated by A. Kukharuk

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Koshlan, T.V., Kulikov, K.G. Analysis of Electrostatic Interaction between Dimer Complexes. Part I: A Method for Selecting Inhibitors of APP Protein Derivatives. Tech. Phys. 65, 1167–1174 (2020).

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