Physical basis for the ofloxacin-induced acceleration of lysozyme aggregation and polymorphism in amyloid fibrils

Archives of Biochemistry and Biophysics
Shivani A MuthuBasir Ahmad

Abstract

Aggregation of globular proteins is an intractable problem which generally originates from partially folded structures. The partially folded structures first collapse non-specifically and then reorganize into amyloid-like fibrils via one or more oligomeric intermediates. The fibrils and their on/off pathway intermediates may be toxic to cells and form toxic deposits in different human organs. To understand the basis of origins of the aggregation diseases, it is vital to study in details the conformational properties of the amyloidogenic partially folded structures of the protein. In this work, we examined the effects of ofloxacin, a synthetic fluoroquinolone compound on the fibrillar aggregation of hen egg-white lysozyme. Using two aggregation conditions (4M GuHCl at pH 7.0 and 37 °C; and pH 1.7 at 65 °C) and a number of biophysical techniques, we illustrate that ofloxacin accelerates fibril formation of lysozyme by binding to partially folded structures and modulating their secondary, tertiary structures and surface hydrophobicity. We also demonstrate that Ofloxacin-induced fibrils show polymorphism of morphology, tinctorial properties and hydrophobic surface exposure. This study will assist in understanding the determinant of...Continue Reading

References

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Jan 29, 2014·Biochimica Et Biophysica Acta·Mohanish S BoranaBasir Ahmad

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Citations

Jan 10, 2021·Scientific Reports·Kathryn P ScherpelzStephen C Meredith
Nov 8, 2020·International Journal of Biological Macromolecules·Aruna K MoraSukhendu Nath
Feb 1, 2020·International Journal of Biological Macromolecules·Kenana Al AdemSungmun Lee
Sep 4, 2019·The Journal of Physical Chemistry. B·Wei FanShilin Liu

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