ArticleScientific reports2026
R5 and R7 positions on fluoroquinolone scaffolds drive F-actin filament disruption.
Article in Scientific reports, 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
8 authors.
Funding
Abstract
Fluoroquinolones (FQs) are widely prescribed broad-spectrum antibiotics, with newer generations capable of crossing the blood brain barrier (BBB). Previous studies have reported the actin-destabilizing effects of FQs, suggesting their potential for drug repurposing. Actin-associated neuropathies are characterised by the formation of persistent, F-actin aggregates in neurons, which impair critical cellular functions. Therefore, identifying small molecules that can disrupt these actin filaments and aggregates can provide a promising therapeutic strategy. This research aims to map the direct interaction between FQs and F-actin to identify the structural basis for actin disruption. We demonstrated that FQs irreversibly disrupt F-actin filaments in a concentration-dependent manner using scattering-based assay. Electron microscopy and gel filtration confirmed generation-dependent disruption activity. In particular, Gen3 and Gen4 FQs reduced actin aggregates in more than 60% yeast cells. FQ treatment altered the thermal stability of F-actin at both 1:30 and 1:50 molar ratios with minor secondary structural changes. To explore the molecular insights of FQs interaction with F-actin, saturation transfer difference-NMR combined with complementary molecular dynamics simulations revealed the importance of the fluorinated quinolone core, which is common to all FQs. These studies highlight the involvement of an amino group at R5, and bulky piperazine, azabicyclo rings at the R7 position in driving F-actin disruption. We would like to propose that rational modifications at R5 and R7 positions can enhance both actin-disrupting potency and BBB permeability, thereby providing a basis for developing FQs derived therapeutics against actin-related neurodegenerative disorders.
Indexed as
Identifiers
What Socratic 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 Socratic graph.