Abstract
Amyloid transformation under laboratory conditions is achieved by shaking an aqueous solution of any protein. The shaking time varies significantly, demonstrating the variable degree of ease of structural transformation in a given protein. The structural specificity that distinguishes amyloid forms from biologically active proteins is the flatness (two-dimensionality) of the form of each chain in the amyloid fibril. The 2D feature, given the globular and therefore 3D structure of biologically active proteins, is an object of analysis in the search for factors favoring amyloid transformation. The use of a modified fuzzy oil drop model (FOD-M) enables this transformation to be mathematically expressed. The mathematical expression is directly related to the shaking conditions, while leaving open the question of an environmental factor under physiological conditions that causes a conformational change resulting in a 2D structure of the polypeptide chain. The examples expressing the environmental prerequisites demonstrated in the current review show the dependence of structuring on the external force field.
Keywords
Amyloid, Transthyretin, VL domain IgG, Synuclein, Enzymes, Hydrophobicity, External force field, Structural changes, Amyloid transformation