Citation: PANG Bo, MENG Xin, BIAN Xin-Yu, LIU Shu, PI Zi-Feng, LIU Zhi-Qiang, SONG Feng-Rui. Interaction Studies of Human Islet Amyloid Polypeptide and Flavonols by Electrospray Ionization-Ion Mobility-Mass Spectrometry and Fluorescence Spectroscopy[J]. Chinese Journal of Analytical Chemistry, ;2021, 49(11): 1881-1889. doi: 10.19756/j.issn.0253-3820.201729 shu

Interaction Studies of Human Islet Amyloid Polypeptide and Flavonols by Electrospray Ionization-Ion Mobility-Mass Spectrometry and Fluorescence Spectroscopy

PANG Bo ^1,2 ,
MENG Xin ^1,2 ,
BIAN Xin-Yu ^1,2 ,
LIU Shu ¹ ,
PI Zi-Feng ¹ ,
LIU Zhi-Qiang ¹ ,
SONG Feng-Rui ^1,,

1.
Jilin Province Key Laboratory of Chinese Medicine Chemistry and Mass Spectrometry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun 130022, China;
2.
School of Applied Chemistry and Engineering, University of Science and Technology of China, Hefei 230029, China

Corresponding author: SONG Feng-Rui, songfr@ciac.ac.cn
Received Date: 4 December 2020
Revised Date: 20 September 2021

Fund Project: Supported by the National Natural Science Foundation of China (Nos.21673219, 81873193).

The interaction of human islet amyloid polypeptide (hIAPP) with five kinds of flavonols (Astragalin, isoquercitrin, isorhamnetin-3-O-neohesperidoside, isorhamnetin-3-O-rutinoside, rutin) was investigated by electrospray ionization-ion mobility-mass spectrometry (ESI-IM-MS) and fluorescence spectroscopy. The results showed that the glycosyl groups and hydroxyl groups of aglycones in flavonols could improve their binding affinity with hIAPP, and enhance the gas phase stability of the complexes formed by hIAPP and ligands. However, the effects of multiple hydroxyl groups of aglycones on IAPP aggregation was more obvious, followed by the number of glycosyl groups and different types of glycosyl groups. Among the five flavonols, the complexes formed by rutin and hIAPP were the most stable and rutin had the strong inhibitory action on the fibrillation of hIAPP. IM-MS analysis results showed that rutin could stabilize the conformation of hIAPP by binding to hIAPP. The obtained results were useful to understand the structure-activity of the interaction of flavonols with hIAPP and provide valuable reference for the screening of potent amyloid inhibitors from natural products.
- Human islet amyloid polypeptide,
- Flavonols,
- Electrospray ionization-ion mobility-mass spectrometry,
- Fluorescence spectroscopy,
- Interaction
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