期刊
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
卷 32, 期 9, 页码 1366-1378出版社
TAYLOR & FRANCIS INC
DOI: 10.1080/07391102.2013.819300
关键词
fibrillation; human serum albumin; Cu(II); stoichiometry; aggregation
资金
- IIT Kharagpur
- CSIR, New Delhi
Protein aggregation is related to a series of pathological disorders the main cause of which are the fibrillar species generated during the process. Human serum albumin (HSA) undergoes rapid fibrillation in the presence of Cu(II) at pH 7.4 in 60% ethanol after 6-h incubation (similar to 65 degrees C) followed by room temperature incubation. Here, we have investigated the effect of a stoichiometric variation of Cu(II) on the self-assembly of HSA using Congo red and thioflavin T dye-binding studies, circular dichroism spectroscopy, Fourier transform infrared spectroscopy, electron paramagnetic resonance spectroscopy, fluorescence microscopy and transmission electron microscopy. The simulation of EPR spectra suggests that with the increment in Cu(II) ion concentration, there is a change in ligand field coordination. Kinetic parameters indicate reduced cooperativity that may be related to the nonspecific coordination on increment of Cu(II) concentration. Cu(II) is also able to direct the accumulation of a large number of fibers along with a formation of dense fibrillar network which is evident from microscopic images.
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