ArticleScientific reports2025
Improved albumin binding properties of Isoguvacine upon esterification as characterized by biophysical and computational tools.
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.
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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.
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Abstract
The prevalence of epilepsy, affecting millions across all age groups, has intensified the need for novel therapeutic interventions. Despite advances in antiseizure medications (ASMs), challenges persist, particularly drug resistance and significant psychiatric and behavioral adverse effects. Isoguvacine (IGV), a potent γ-aminobutyric acid type A receptor agonist, holds promise for epilepsy treatment but suffers from poor blood-brain barrier (BBB) permeability due to its zwitterionic nature. To address this limitation, two ester prodrugs: E7 (heptyl 1,2,3,6-tetrahydropyridine-4-carboxylate) and E14 (tetradecyl 1,2,3,6-tetrahydropyridine-4-carboxylate) were synthesized to enhance BBB penetration and central nervous system (CNS) delivery. This study investigates the interactions of IGV and its derivatives with human serum albumin (HSA), a key plasma transport protein, using a suite of biophysical and computational techniques. UV spectroscopic analysis confirmed protein-ligand complexation, with E7 and E14 exhibiting enhanced binding compared to IGV. Isothermal titration calorimetry revealed that E14 demonstrated superior binding affinity (K
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