ArticleScientific reports2025
Insights into the interaction of Fibrinogen with Timolol Maleate and elucidation of binding sites via. spectroscopic and molecular docking study.
Article in Scientific reports, 2025. 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
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Timolol maleate (TM), a beta-blocker drug, is used in treating conditions related to arterial hypertension. Exploring the possible interaction between TM and plasma proteins is crucial for enhancing the drug potency. This interaction study is done to examine the impact of TM on the comportment of bovine plasma Fibrinogen (FB) by utilizing spectroscopic and computational techniques such as fluorescence spectroscopy, circular dichroism (CD), and molecular docking. Employing fluorescence spectroscopy at temperatures 290 K, 298 K, and 308 K disclosed that TM used hydrophobic interactions to quench the intrinsic fluorescence of FB and show a hypochromic shift. The values of the binding and quenching rate constant specify the strong interaction between the TM and FB. The thermodynamic parameters such as ΔH and ΔG unveil the existence of hydrophobic forces. The CD demonstrates the influence of TM on the secondary structure of FB. Molecular docking revealed the theoretical evaluation of FB and TM binding. The investigation provides insightful information on stability, pharmacokinetics and bioavailability of TM, which is crucial for maximizing its therapeutic value.
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.