Protein amyloids develop an intrinsic fluorescence signature during aggregation.
Protein amyloids develop an intrinsic fluorescence signature during aggregation.
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DOI：
10.1039/c3an36798c
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发表时间：
2013-04-07
期刊：
影响因子：
--
通讯作者：
Kaminski CF
中科院分区：
文献类型：
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作者：
Chan FT;Kaminski Schierle GS;Kumita JR;Bertoncini CW;Dobson CM;Kaminski CF
我们报告了在可见光范围内观察到的本征荧光，它在一系列多肽的聚集过程中产生，包括与疾病相关的人类多肽-β(1-40)和(1-42)、溶菌酶和tau。实验测定了其发射寿命和光谱等特征荧光性质。这种本征荧光与多肽结构中芳香族侧链残基的存在无关。相反，它似乎是由于多肽链折叠成交叉β片状支架时可用的电子水平造成的，类似于已报道的在晶体中发生的情况。我们利用这些发现通过荧光成像以一种无标记的方式来量化体外蛋白质聚集。
We report observations of an intrinsic fluorescence in the visible range, which develops during the aggregation of a range of polypeptides, including the disease-related human peptides amyloid-β(1–40) and (1–42), lysozyme and tau. Characteristic fluorescence properties such as the emission lifetime and spectra were determined experimentally. This intrinsic fluorescence is independent of the presence of aromatic side-chain residues within the polypeptide structure. Rather, it appears to result from electronic levels that become available when the polypeptide chain folds into a cross-β sheet scaffold similar to what has been reported to take place in crystals. We use these findings to quantify protein aggregation in vitro by fluorescence imaging in a label-free manner.