Abstract Title:

Myricetin inhibits amyloid fibril formation of globular proteins by stabilizing the native structures.

Abstract Source:

Colloids Surf B Biointerfaces. 2019 Nov 11 ;186:110640. Epub 2019 Nov 11. PMID: 31835184

Abstract Author(s):

Kailash P Prajapati, Akhilesh P Singh, Kriti Dubey, Masihuzzaman Ansari, Mayur Temgire, Bibin G Anand, Karunakar Kar

Article Affiliation:

Kailash P Prajapati


Myricetin has been identified as a naturally occurring flavonoid class of polyphenolic compound which shows multiple medical benefits including antidiabetic, anticancerous and antioxidant properties. Here, we report the protective effect of myricetin against in vitro amyloid fibril formation of selected globular proteins. The results reveal that myricetin is capable of inhibiting amyloid fibril formation of both insulin and serum albumin. Seed-induced aggregation of both proteins was also substantially suppressed in the presence of myricetin. Fluorescence quenching data indicated binding of myricetin with protein monomers as well as fibrils. The molecular docking studies revealed strong affinity of myricetin for both the native and partially unfolded conformation of proteins mediated by H-bonds and hydrophobic interactions. Myricetin was also observed to promote disassembly of mature amyloid fibrils. The results reveal that myricetin molecule has the potential for suppressing amyloid formation and such an inherent property may help in developing myricetin-based antiamyloid drugs.

Study Type : In Vitro Study

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