Abstract

Human serum albumin (HSA) is a natural buffer for amyloid в peptide (Аβ), which is a key factor in the development of Alzheimer's disease (AD). An increase in HSA affinity to Аβ can be achieved via HSA saturation with low-molecular-weight ligands, such as serotonin or specific fatty acids. The conducted analysis of the genomic data of exomes (WES) associated with AD (ADSP database) revealed the presence of a single-nucleotide polymorphism of the HSA gene at the binding sites of ibuprofen, arachidonic and oleic acids. Research into the properties of the revealed genetic variants of HSA should be carried out to determine those variants that are susceptible to the modulatory action of HSA ligands, thus increasing its affinity to Aβ.

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