ArticleAdvanced pharmaceutical bulletin2026
Psoralen and Seselin Stabilize the α-helix Structure in Lysozyme and Inhibit the α-helix to β-sheet Exchange: An Efficient Anti-Amyloidogenic Mechanism.
Article in Advanced pharmaceutical bulletin, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Purpose: More than thirty human proteins have natural propensity to misfold and amyloid fibril formation that are important in the initiation and development of neurodegenerative disease. Therefore, preventing or reversing amyloid aggregation by using drugs or plant-based small molecules such as coumarin compounds could be useful. This study aimed to investigate the anti-amyloidogenic potential of psoralen and seselin, two types of coumarin compounds, on hen egg white lysozyme (HEWL) as a model system. Method: ThioflavinT (ThT), Congo red and ANS fluorescence, electron microscopy and circular dichroism were used to fibrillogenesis assay and structural analysis in the presence and absence of the compounds. Interaction of HEWL and coumarins evaluated by using surface plasmon resonance (SPR) and molecular docking and simulation. Results: The results indicated the ThT and ANS fluorescence intensities decreased in the presence of psoralen and seselin in a dose-dependent dependent manner, suggesting a strong inhibitory effect of compounds on HEWL fibril formation. The results confirmed coumarins could destabilize the pre-formed fibrils. Furthermore, Fluorescence analysis confirmed that coumarin interaction induces conformational changes in HEWL, evidenced by formation of non-fluorescent complexes and altered microenvironments around Tyr and Trp residues. CD spectrum revealed that coumarins can inhibit the α-helix to β-sheet exchange. SPR results showed psoralen could bind to HEWL more tightly. Conclusion: In agreement with experimental results, the molecular docking studies confirmed the conformational changes of HEWL upon interaction with psoralen and seselin. This study adds to the body of knowledge about rational drug design against the amyloidogenesis process.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.