Detecting the inter-peptide arrangement and maturation process of transthyretin (105-115) amyloid fibril using a FRET pair with short Förster distance.
Detecting the inter-peptide arrangement and maturation process of transthyretin (105-115) amyloid fibril using a FRET pair with short Förster distance.
复制标题
使用短福斯特距离的 FRET 对检测转甲状腺素蛋白 (105-115) 淀粉样原纤维的肽间排列和成熟过程。
DOI：
10.1016/j.bbrc.2007.08.059
复制
发表时间：
2007
影响因子：
3.1
通讯作者：
L. Lai
中科院分区：
文献类型：
--
作者：
W. Deng;Aoneng Cao;L. Lai
甲状腺素运载蛋白（TTR）是一种淀粉样蛋白，与许多精神疾病有关。来源于TTR（105-115）的肽已作为理解淀粉样蛋白原纤维形成机制的模型肽被广泛研究。然而，这种肽在淀粉样纤维中的详细排列仍不清楚。我们通过在TTR（105-115）的N-末端带有丹磺酰基、C-末端带有色氨酸残基的肽段中引入一对FRET探针，研究了TTR（105-115）的淀粉样纤维形成过程。我们的实验表明，在淀粉样蛋白原纤维中，TTR（105-115）在同一β-折叠中的链可能是平行的，而配对的折叠可能是相互反平行的。FRET和EM的动力学表明，一个可能的中间状态和片之间的距离变得更短时，中间淀粉样蛋白原纤维变成一个更成熟的形式。
Transthyretin (TTR) is an amyloidogenic protein involved in many mental diseases. The peptide derived from TTR (105–115) has been widely studied as a model peptide for understanding the mechanism of amyloid fibril formation. However, the detailed arrangement of this peptide in amyloid fibril is still unclear. We have studied the amyloid fibril formation process of TTR (105–115) by introducing a pair of FRET probes into the peptide with a dansyl group at the N-terminal and a tryptophan residue at the C-terminal. Our experiment demonstrated that the strands of TTR (105–115) in the same β-sheet may be parallel and the mating sheets may be anti-parallel to each other in the amyloid fibril. The kinetics followed by FRET and EM indicated for a possible intermediate state and the distance between sheets became shorter when the intermediate amyloid fibril turns into a more matured form.