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A quercetin-based flavanoid (rutin) reverses amyloid fibrillation in β-lactoglobulin at pH 2.0 and 358 K
Al-Shabib, Nasser Abdulatif, Al-Shabib N.A, Khan J.M, Malik A, Alsenaidy M.A, Husain F.M, Alsenaidy A.M, Khan R.H, Choudhry H, Zamzami M.AShow More
Published in Elsevier BV
PMID: 30763917
Volume: 214
Pages: 40 - 48
β-lactoglobulin (BLG) is a well characterized milk protein and a model for folding and aggregation studies. Rutin is a quercetin based-flavanoid and a famous dietary supplement. It is a potential protector from coronary heart disease, cancers, and inflammatory bowel disease. In this study, amyloid fibrillation is reported in BLG at pH 2.0 and temperature 358 K. It is inhibited to some extent by rutin with a rate of 99.3 h −1 M −1 . Amyloid fibrillation started taking place after 10 h of incubation and completed near 40 h at a rate of 16.6 × 10 −3 h −1 , with a plateau during 40–108 h. Disruption of tertiary structure of BLG and increased solvent accessibility of hydrophobic core seem to trigger intermolecular assembly. Increase in 7% β-sheet structure at the cost of 10% α-helical structures and the electron micrograph of BLG fibrils at 108 h further support the formation of amyloid. Although it could not block amyloidosis completely, and even the time required to reach plateau remains the same, a decrease of growth rate from 16.6 × 10 −3 to 13.5 × 10 −3 h −1 was observed in the presence of 30.0 μM rutin. Rutin seems to block solvent accessibility of the hydrophobic core of BLG. A decrease in the fibril population was observed in electron micrographs, with the increase in rutin concentration. All evidences indicate reversal of fibrillation in BLG in the presence of rutin. © 2019 Elsevier B.V.
About the journal
JournalData powered by TypesetSpectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
PublisherData powered by TypesetElsevier BV
Open Access0