Abstract

Proteins in neurodegenerative diseases (NDs) frequently accumulate and are misfolded. There is treatment for NDs, and the molecular processes that lead to this pathological aggregation have been extensively studied. Fibrillary deposits of -synuclein (-Syn), a protein that is thermostable and highly conserved, exacerbate neurodegenerative diseases (NDs) like Alzheimer's, Parkinson's, and Lewy body. As a result, inhibiting -Syn aggregation may be an option for therapeutic treatment. The debasement of target proteins by microscopic particles has gained interest in drug research in recent years as yet another useful method. Functional foods and dietary supplements derived from food's bioactive compounds are also gaining popularity as ND intervention agents. Reports propose that dietary bioactive phospholipids might further develop cognizance and defend neurons because of their capacity to impact psychological wellness and comprehension in vivo and in vitro. However, it is necessary to clarify the mechanisms by which lipids may prevent the pathological aggregation of -Syn. Our investigation of the evidence for the potential instruments that underpin this effect focuses primarily on PLDP-inferred lysophospholipids (LPLs), which have the potential to limit - Syn collection.

Keywords: Lysophospholipids; Neurodegenerative Diseases; Amyloid; Α-Synuclein