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- W4381949485 abstract "Amyloidopathies are associated with a biochemical change in concerned organ or bio-environment known as inflammation (promoted in case of fibrils accumulation due to their stability) that triggered us to explore anti-aggregating and disaggregating property of an anti-inflammatory drug amodiaquine (AD) against human lysozyme (HL) fibrillation in this study simultaneously evaluating the mechanism of interaction between AD and HL using biophysical and microscopic techniques. The linear modified Stern-Volmer plot obtained from fluorescence quenching of HL by AD at three temperatures and Ksv dependence on temperature with kq > 2.0 × 1010 supports static quenching mechanism with strong binding (Kb = × 106) and negative ΔG value. The change in Trp and Tyr environment due to AD binding were confirmed via synchronous fluorescence. The studies were further extended to analyse aggregation inhibition and disaggregation of HL by AD. RLS, ThT, CD and DLS results suggested aggregation inhibition and disaggregation which was further confirmed via TEM. Overall, our study suggests that AD is an effective drug for fibrillation inhibition and disaggregation. The possible mechanism behind this behaviour is the stabilization of HL in native state by AD via non-covalent interactions and thus AD will not only reduce fibril burden but will also calm severity of the disease (such as regaining cognitive function due to reduced inflammation). This can be an alternative promising approach that can be exploited for treating amyloidopathies such as Alzheimer’s, Parkinson’s disease and systemic amyloidosis." @default.
- W4381949485 created "2023-06-26" @default.
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- W4381949485 date "2023-09-01" @default.
- W4381949485 modified "2023-09-29" @default.
- W4381949485 title "Revelation of anti-aggregating and disaggregating characteristic of amodiaquine via inhibition of human lysozyme fibrillation: Therapeutic alternative for treating amyloidopathies" @default.
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- W4381949485 doi "https://doi.org/10.1016/j.molliq.2023.122438" @default.
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