Nanoscale Structural Analysis of a Lipid-Driven Aggregation of Insulin.
Nanoscale Structural Analysis of a Lipid-Driven Aggregation of Insulin.
复制标题
脂质驱动的胰岛素聚集的纳米级结构分析。
DOI:
10.1021/acs.jpclett.1c04012
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发表时间:
2022-03-17
影响因子:
5.7
通讯作者:
Kurouski, Dmitry
中科院分区:
文献类型:
--
作者:
Rizevsky, Stanislav;Matveyenka, Mikhail;Kurouski, Dmitry
Abrupt aggregation of misfolded proteins is a hallmark of a large number of severe pathologies, including diabetes types 1 and 2, Alzheimer, and Parkinson diseases. A growing body of evidence suggests that lipids can uniquely change rates of amyloid-associated proteins as well as modify the structure of formed oligomers and fibrils. In this study, we utilize atomic force microscopy infrared (AFM-IR) spectroscopy, also known as nano-IR spectroscopy, to examine the structure of individual insulin oligomers, protofilaments, and fibrils grown in the presence of phospholipids. Our findings show that AFM-IR spectra of insulin oligomers have strong signals of C–H and PO2− vibrations, which points on the presence of lipids in the oligomer structure. Furthermore, substantial shifts in lipid vibrations in AFM-IR spectra of the oligomers relative to the corresponding bands of pure lipids have been observed. This points on strong interactions between a lipid and a protein that are developed at the stage of the oligomer formation.
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DOI:
10.1073/pnas.1421204112
发表时间:
2015-04-21
影响因子:
11.1
作者:
Chen, Serene W.;Drakulic, Srdja;Cremades, Nunilo
通讯作者:
Cremades, Nunilo
影响因子:
7.4
作者:
Katzenmeyer, Aaron M.;Holland, Glenn;Centrone, Andrea
通讯作者:
Centrone, Andrea
DOI:
10.1093/jnen/61.5.413
发表时间:
2002-05-01
影响因子:
3.2
作者:
Del Tredici, K;Rüb, U;Braak, H
通讯作者:
Braak, H
影响因子:
3.9
作者:
Kochan, Kamila;Perez-Guaita, David;Wood, Bayden R.
通讯作者:
Wood, Bayden R.
影响因子:
7.4
作者:
Katzenmeyer, Aaron M.;Aksyuk, Vladimir;Centrone, Andrea
通讯作者:
Centrone, Andrea