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Int J Biol Macromol. 2017 Feb;95:713-718. doi: 10.1016/j.ijbiomac.2016.11.110. Epub 2016 Dec 2.

Attenuation of amyloid fibrillation in presence of Warfarin: A biophysical investigation.

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Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, 202002, Uttar Pradesh, India.
Molecular Biology Department, Genetic Engineering and Biotechnology Division, National Research Centre, Dokki, Cairo, Egypt.
Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, 202002, Uttar Pradesh, India. Electronic address:


Protein misfolding and aggregation are associated with more than twenty diseases, such as neurodegenerative diseases. The amyloid oligomers and fibrils may induce cell membrane disruption and lead to cell apoptosis. A great number of studies have focused on discovery of amyloid inhibitors which may prevent or treat amyloidosis. In this study, we used human serum albumin (HSA) as an amyloid model to test the anti-amyloid effects of warfarin (WFN), a very well-known drug for treatment of thrombosis and also used by biophysicists to characterize the specific binding site on HSA (site I of subdomain IIA). We have used a combination of different biophysical, spectroscopic and imaging techniques to prove the anti-amyloidogenic behavior of WFN. Our results demonstrated that WFN is capable enough to inhibit the HSA fibrillation. Exposed HSA surface hydrophobicity was decreased by 50% as judged by ANS analysis. Moreover, anti-amyloidegenic behavior of WFN was found to be concentration dependent as supported by decreased ThT fluorescence by 22.4% and 46% at WFN concentrations of 500 and 1000μM, respectively. Circular dichroism technique showed the change in secondary structure of native HSA as well as in presence of WFN. These results suggests that WFN is capable of inhibiting amyloid aggregation, hence, WFN related compounds may thus be further explored for designing effective anti-amyloidosis compounds.


Aggregation inhibition; Amyloid fibrils; Amyloidosis; Beta sheet conformation; Congo red binding; ThT binding

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