2019
DOI: 10.1002/jms.4463
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Study of the noncovalent interactions of ginsenosides and amyloid‐β‐peptide by CSI‐MS and molecular docking

Abstract: Noncovalent interactions between drugs and proteins play significant roles for drug metabolisms and drug discoveries. Mass spectrometry has been a commonly used method for studying noncovalent interactions. However, the harsh ionization process in electrospray ionization mass spectrometry (ESI-MS) is not conducive to the preservation of noncovalent and unstable biomolecular complexes compared with the cold spray ionization mass spectrometry (CSI-MS). A cold spray ionization providing a stable solvation-ionizat… Show more

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Cited by 6 publications
(2 citation statements)
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“…Amyloid β (Aβ) peptide plays an important role in AD. Zhou et al reported that Re may interfere with AD progression by affecting the Aβ peptide ( Zhou et al, 2020 ). Oral administration of Re (25 mg/kg, i.g.…”
Section: Pharmacological Effects Of Re On Nervous Diseasesmentioning
confidence: 99%
“…Amyloid β (Aβ) peptide plays an important role in AD. Zhou et al reported that Re may interfere with AD progression by affecting the Aβ peptide ( Zhou et al, 2020 ). Oral administration of Re (25 mg/kg, i.g.…”
Section: Pharmacological Effects Of Re On Nervous Diseasesmentioning
confidence: 99%
“…A variant of ESI‐MS, called cold spray ionisation mass spectrometry (CSI‐MS) is an alternative method. It proved to be a milder and less destructive method, advantageous when studying non‐covalent drug‐protein stoichiometries, and thus could be a more appropriate approach for many aspects of Aβ therapeutics research (Jiang et al, 2019; Zhou et al, 2020).…”
Section: Tools For Analysismentioning
confidence: 99%