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Structural and Pharmacological Insights into Propranolol: An Integrated Crystallographic Perspective

Adrianna Witczyńska, Łukasz Fijałkowski, Dagmara Mirowska-Guzeł, Kamilla Blecharz‐Klin, Alicja Nowaczyk

2025International Journal of Molecular Sciences7 citationsDOIOpen Access PDF

Abstract

Propranolol is a non-selective β-adrenergic receptor antagonist widely used in cardiovascular and neurological therapy. Its naphthalene-based structure contributes to its high lipophilicityand central nervous system penetration. Clinically, propranolol is indicated for hypertension, arrhythmias, anxiety, migraine, and other conditions. It undergoes extensive hepatic metabolism via cytochrome P450 enzymes, notably CYP2D6, with a significant first-pass effect limiting oral bioavailability. This review integrates pharmacological profiling with crystallographic analysis to explore propranolol’s molecular interactions and therapeutic versatility. High-resolution crystal structures of the human β2-adrenergic receptor (hβ2-AR), particularly PDB ID: 6PS5 obtained via serial femtosecond crystallography (SFX), reveal key binding determinants responsible for receptor affinity and antagonism. Comparative structural analysis with other β-blockers—alprenolol, timolol, and carvedilol—highlights how variations in aromatic and heterocyclic frameworks influence pharmacokinetics and receptor selectivity. Superimposition results (RMSD: 0.032 for propranolol–alprenolol, 0.078 for propranolol–carvedilol, and 1.078 for propranolol–timolol) quantitatively illustrate molecular similarity and divergence. The enantioselective behavior of propranolol is also discussed, with the S-enantiomer showing greater receptor affinity and pharmacological potency than the R-form. Beyond canonical β-adrenergic targets, propranolol interacts with non-canonical proteins such as the cellulase enzyme Cel7A and lactoferrin, suggesting off-target effects and novel therapeutic potential. These findings underscore the importance of propranolol’s amphiphilic character, stereochemistry, and electrostatic properties in shaping its pharmacological profile. Overall, the integration of crystallographic data with pharmacological insights supports the rational design of next-generation β-adrenergic ligands with enhanced selectivity, bioavailability, and clinical efficacy.

Topics & Concepts

PropranololChemistryDocking (animal)ReceptorRational designMolecular dynamicsProtein Data Bank (RCSB PDB)StereochemistryPharmacologyProtein structureMolecular modelStructural similarityComputational biologyBiochemistryPlasma protein bindingCytochrome P450Drug discoveryStructure–activity relationshipHomology modelingBinding sitePharmacokineticsBiophysicsDrug designBioinformaticsAntagonistProtein subunitEnantiomerG protein-coupled receptorCrystal structureLigand (biochemistry)Crystallization and Solubility StudiesAnalytical Chemistry and ChromatographyComputational Drug Discovery Methods