Fibrillation in Human Serum Albumin Is Enhanced in the Presence of Copper(II)
The Journal of Physical Chemistry B2010Vol. 114(31), pp. 10228–10233
Citations Over TimeTop 18% of 2010 papers
Abstract
The aggregation process in proteins is governed by several factors such as temperature, pH, presence of electrolytes, denaturants, and metal ions. Here, we report the role of Cu(II) in inducing rapid fibrillation in human serum albumin. We have monitored this process via UV-vis spectroscopy, fluorescence spectroscopy, circular dichroism, zeta-potential measurements, electron paramagnetic resonance studies, fluorescence microscopy, and field emission scanning electron microscopy. Images show a fibrillar network of human serum albumin in the presence of Cu(II) in 60% ethanol incubated at 65 degrees C at physiological pH. All other studies also support the enhanced fibrillation in presence of Cu(II).
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