Abstract:
:The 129-residue lysozyme has been shown to form amyloid fibrils in vitro. While methylene blue (MB), a compound in the phenothiazinium family, has been shown to dissemble tau fibril formation, its anti-fibrillogenic effect has not been thoroughly characterized in other proteins/peptides. This study examines the effects of MB on the in vitro fibrillogenesis of lysozyme at pH 2.0 and 55 °C. Our results demonstrated that, upon 7-day incubation, the plateau ThT fluorescence of the sample was found to be ~8.69% or ~2.98% of the control when the molar ratio of lysozyme to MB was at 1:1.11 or 1:3.33, respectively, indicating that the inhibitory potency of MB against lysozyme fibrillogenesis is positively correlated with its concentration. We also found that MB is able to destabilize the preformed lysozyme fibrils. Moreover, molecular docking and molecular dynamics simulations results revealed that MB's mechanism of fibril formation inhibition may be triggered by binding with lysozyme's aggregation-prone region. Results reported here provide solid support for MB's effect on amyloid fibrillogenesis. We believe the additional insights gained herein may pave way to the discovery of other small molecules that may have similar action toward amyloid fibril formation and its associated diseases.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
How SC,Cheng YH,Lo CH,Lai JT,Lin TH,Bednarikova Z,Antosova A,Gazova Z,Wu JW,Wang SSdoi
10.1016/j.ijbiomac.2018.08.038subject
Has Abstractpub_date
2018-11-01 00:00:00pages
1059-1067eissn
0141-8130issn
1879-0003pii
S0141-8130(18)32680-1journal_volume
119pub_type
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