Abstract
Formation of amyloid fibrils from an amyloidogenic precursor peptide is a stochastic process. Initially, conditions do not favor aggregation, and this period corresponds to the lag phase that precedes the possible formation of fibrils. This lag phase can be overcome by the amyloidogenic peptide reaching a critically high concentration, or via binding with apolipoproteins or other chaperone proteins. Apolipoproteins interact with numerous amyloidogenic peptides in diverse systemic and organ limited amyloidoses because of their natural tendency to bind hydrophobic domains present on these peptides. Apolipoproteins appear to play an essential role in the kinetics of amyloid deposition. Apoliprotein E (apo E), which has been found to be involved in the majority of amylodoses, helps to overcome the initially unfavorable kinetic barrier of amyloid fibril formation, and typically shows isoform-specific effects that influence the epidemiology, clinical course, and pathological aspects of disease. The modulatory effect of apolipoproteins may not be evident if either the amyloid-prone protein is present in great excess or carries a mutation rendering it extremely amyloidogenic. Under these conditions amyloid deposition can occur without the help of chaperones. The exact binding site of amyloidogenic peptides on apo E and other apolipoproteins is unclear, and it remains unknown if it is a linear or a conformational epitope. Mapping this site could provide a means to clarify the mechanism of interaction between apolipoproteins and their peptide ligands, as well as allowing the generation of peptidomimetic compounds that block this interaction in an effort to develop successful treatment approaches. It appears that apo E has one universal site interacting with various amyloidogenic peptides regardless of their sequence. Targeting the pathological chaperones of amyloidoses such as apo E appears to be an attractive approach from a pharmacokinetic point of view, because the concentration of these molecules in amyloid deposits is usually 100 to 200 times lower than the concentration of the actual fibril-forming peptide (Ma et al., 1994; Wisniewski et al., 1994a). In addition, blocking this interaction between apo E and amyloidogenic proteins is unlikely to be associated with any significant toxicity, making this a significant therapeutic target.
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Sadowski, M., Wisniewski, T. (2006). Apolipoproteins in Different Amyloidoses. In: Uversky, V.N., Fink, A.L. (eds) Protein Misfolding, Aggregation, and Conformational Diseases. Protein Reviews, vol 4. Springer, Boston, MA. https://doi.org/10.1007/0-387-25919-8_6
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