Screening apo-SOD1 conformation stabilizers from natural flavanones using native ion mobility mass spectrometry and fluorescence spectroscopy methods.
Bing ZhaoXinyu BianXiaoyu ZhuangShu LiuZhiqiang LiuFengrui SongPublished in: Rapid communications in mass spectrometry : RCM (2022)
This study revealed that the binding of liquiritin apioside can stabilize apo-SOD1 dimer and inhibit the aggregation of apo-SOD1, and illustrated that native ESI-IM-MS is a powerful tool for providing insight into investigating the structure-activity relationship between small molecules and protein, and screening protein conformation stabilizers.
Keyphrases
- mass spectrometry
- amyotrophic lateral sclerosis
- ms ms
- high resolution
- single molecule
- binding protein
- protein protein
- molecular dynamics simulations
- liquid chromatography
- multiple sclerosis
- amino acid
- crystal structure
- high performance liquid chromatography
- single cell
- small molecule
- transcription factor
- energy transfer