期刊
PHYSICAL BIOLOGY
卷 9, 期 5, 页码 -出版社
IOP PUBLISHING LTD
DOI: 10.1088/1478-3975/9/5/056005
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资金
- National Science Foundation Materials Research Science and Engineering Centers program [DMR 1120296, DMR 0520404]
- National Institute of Health [5 R21 AG026650, AG019391, AG025440]
- National Science Foundation STC program [ECS-9876771]
- Irma T Hirschl Foundation
Both increased temperature and moderate concentrations of fluorinated alcohols enhance aggregation of the Parkinson's disease-associated protein alpha-synuclein (alpha S). Here, we investigate the secondary structural rearrangements induced by heating and trifluoroethanol [TFE]. At low TFE concentrations, CD spectra feature a negative peak characteristic of disordered polypeptides near 200 nm and a slight shoulder around 220 nm suggesting some polyproline-II content. Upon heating, these peaks weaken, while a weak negative signal develops at 222 nm. At high TFE concentrations, the spectra show distinct minima at 208 and 222 nm, indicative of considerable alpha-helical structure, which diminish upon heating. We observe a crossover between the low-TFE and high-TFE behavior near 15% TFE, where we previously showed that a partially helical intermediate is populated. We postulate that the protein is well solvated by water at low TFE concentrations and by TFE at high TFE concentrations, but may become desolvated at the crossover point. We discuss the potential roles and interplay of desolvation and helical secondary structure in driving alpha S aggregation.
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