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Issue 48, 2019
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Distinctively complete inhibition of fibrillation of serum albumins by methotrexate in vitro: experimental and modelling studies to understand the tuning of protein misfolding-related aggregations

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Abstract

Observation of apparently never-ending lag-phase in the fibrillation of serum albumins (SAs) with low concentration of methotrexate (MTX) appears very promising and quite unique for clinical implications toward prevention of aggregation-related disorders. In the present work, we showcase that thermally induced bovine serum albumin (BSA) and human serum albumin (HSA) fibrillation is significantly inhibited by folic acid (FA), and completely by MTX. Surflex-docking, molecular dynamics (MD) simulation and aggregation-propensity studies provide a molecular level scenario that justifies the longer lag-phase in kinetics or high suppression of fibrillation by drugs.

Graphical abstract: Distinctively complete inhibition of fibrillation of serum albumins by methotrexate in vitro: experimental and modelling studies to understand the tuning of protein misfolding-related aggregations

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Publication details

The article was received on 11 Oct 2019, accepted on 18 Nov 2019 and first published on 18 Nov 2019


Article type: Letter
DOI: 10.1039/C9NJ05128G
New J. Chem., 2019,43, 18983-18987

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    Distinctively complete inhibition of fibrillation of serum albumins by methotrexate in vitro: experimental and modelling studies to understand the tuning of protein misfolding-related aggregations

    D. K. Khatua and M. Halder, New J. Chem., 2019, 43, 18983
    DOI: 10.1039/C9NJ05128G

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