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Abstract Title:

Self-Assembly of Artificial Sweetener Aspartame Yields Amyloid-like Cytotoxic Nanostructures.

Abstract Source:

ACS Nano. 2019 May 28 ;13(5):6033-6049. Epub 2019 May 6. PMID: 31021591

Abstract Author(s):

Bibin Gnanadhason Anand, Kailash Prasad Prajapati, Kriti Dubey, Naseem Ahamad, Dolat Singh Shekhawat, Pramod Chandra Rath, George Kodimattam Joseph, Karunakar Kar

Article Affiliation:

Bibin Gnanadhason Anand

Abstract:

Recent reports have revealed the intrinsic propensity of single aromatic metabolites to undergo self-assembly and form nanostructures of amyloid nature. Hence, identifying whether aspartame, a universally consumed artificial sweetener, is inherently aggregation prone becomes an important area of investigation. Although the reports on aspartame-linked side effects describe a multitude of metabolic disorders, the mechanistic understanding of such destructive effects is largely mysterious. Since aromaticity, an aggregation-promoting factor, is intrinsic to aspartame's chemistry, it is important to know whether aspartame can undergo self-association and if such a property can predispose any cytotoxicity to biological systems. Our study finds that aspartame molecules, under mimicked physiological conditions, undergo a spontaneous self-assembly process yielding regularβ-sheet-like cytotoxic nanofibrils of amyloid nature. The resultant aspartame fibrils were found to trigger amyloid cross-seeding and become a toxic aggregation trap for globular proteins, Aβ peptides, and aromatic metabolites that convert native structures to β-sheet-like fibrils. Aspartame fibrils were also found to induce hemolysis, causing DNA damage resulting in both apoptosis and necrosis-mediated cell death. Specific spatial arrangement between aspartame molecules is predicted to form a regular amyloid-like architecture with a sticky exterior that is capable of promoting viable H-bonds, electrostatic interactions, and hydrophobic contacts with biomolecules, leading to the onset of protein aggregation and cell death. Results reveal that the aspartame molecule is inherently amyloidogenic, and the self-assembly of aspartame becomes a toxic trap for proteins and cells, exposing thebitter side of such a ubiquitously used artificial sweetener.

Study Type : Animal Study
Additional Links
Additional Keywords : Risk Factors : CK(3057) : AC(392)
Problem Substances : Aspartame : CK(135) : AC(47)

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