期刊
CHEMICAL COMMUNICATIONS
卷 47, 期 38, 页码 10686-10688出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c1cc14230e
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-
资金
- Polish Ministry of Education and Science [NN 301 101236]
Thioflavin T (ThT) is a molecular-rotor-type fluorophore reputed for the selective binding to amyloid fibrils. Using induced circular dichroism, here we show that ThT binds in an orderly manner to alpha-helical poly-L-glutamic acid (PLGA) implying that neither stacked beta-sheets nor pi-pi stacking interactions are necessary for the binding between the dye and proteins.
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