Journal
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
Volume 39, Issue 12, Pages 4279-4289Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/07391102.2020.1775701
Keywords
Human gamma D-crystallin; morin; fibrillation inhibition; fluorescence quenching; three-dimensional fluorescence; excited state life time
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The study found that morin effectively inhibits the formation of amyloid fibrils by human gamma D-crystallin, demonstrating potential therapeutic value for related diseases. Interaction between HGD and morin involves hydrogen bonding and/or van der Waals forces, supported by docking predictions.
To inhibit the formation of amyloid fibrils by human gamma D-crystallin (HGD), a series of four flavonoids (quercertin, rutin, morin and hesperetin) was tested. Only morin had demonstrated significant inhibition of HGD fibrillation. Results from fluorimetric assay techniques (using thioflavin T and ANS), FTIR, circular dichroism and microscopic imaging (fluorescence microscopy and transmission electron microscopy) confirmed HGD fibrillation inhibition by morin. HGD-morin complex formation at ground state resulted tryptophan fluorescence quenching through static mechanism, which was also confirmed by determining the excited-state life time of HGD tryptophan residues. Forster resonance energy transfer occurs from HGD to morin. Synchronous, three-dimensional fluorescence, FTIR and circular dichroism results suggest that major changes in HGD conformation did not occur on binding with morin. The interactions between HGD and morin involve hydrogen bonding and/or van der Waals forces. Docking predictions also support experimental results.
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