共 50 条
Alpha Synuclein Fibrils Contain Multiple Binding Sites for Small Molecules
被引:56
|作者:
Hsieh, Chia-Ju
[1
]
Ferrie, John J.
[2
]
Xu, Kuiying
[1
]
Lee, Iljung
[1
]
Graham, Thomas J. A.
[1
]
Tu, Zhude
[3
]
Yu, Jennifer
[4
]
Dhavale, Dhruva
[4
]
Kotzbauer, Paul
[4
]
Petersson, E. James
[2
]
Mach, Robert H.
[1
]
机构:
[1] Univ Penn, Perelman Sch Med, Dept Radiol, Philadelphia, PA 19104 USA
[2] Univ Penn, Dept Chem, Philadelphia, PA 19104 USA
[3] Washington Univ, Mallinckrodt Inst Radiol, Sch Med, St Louis, MO 63110 USA
[4] Washington Univ, Dept Neurol, Sch Med, St Louis, MO 63110 USA
来源:
基金:
美国国家卫生研究院;
关键词:
Alpha synuclein;
Lewy bodies;
Lewy neurites;
Parkinson's disease;
ALZHEIMERS-DISEASE;
PARKINSONS-DISEASE;
TAU;
INCLUSIONS;
DESIGN;
BETA;
D O I:
10.1021/acschemneuro.8b00177
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
The fibrillary aggregation of the protein alpha synuclein (Asyn) is a hallmark of Parkinson's disease, and the identification of small molecule binding sites on fibrils is essential to the development of diagnostic imaging probes. A series of molecular modeling, photoaffinity labeling, mass spectrometry, and radioligand binding studies were conducted on Asyn fibrils. The results of these studies revealed the presence of three different binding sites within fibrillar Asyn capable of binding small molecules with moderate to high affinity. A knowledge of the amino acid residues in these binding sites will be important in the design of high affinity probes capable of imaging fibrillary species of Asyn.
引用
收藏
页码:2521 / 2527
页数:13
相关论文