Allosteric binding cooperativity in a kinetic context

Allosteric modulators are of prime interest in drug discovery. These drugs regulate the binding and function of endogenous ligands, with some advantages over orthosteric ligands. A typical pharmacological parameter in allosteric modulation is binding cooperativity. This property can yield unexpected...

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Detalles Bibliográficos
Autores: Díaz Sanzo, Óscar|||0000-0002-8374-1693, Martín, Victor, Renault de Barros, Pedro Victor|||0000-0002-5649-3057, Romero i Sànchez, David|||0000-0002-2881-268X, Guillamon, Antoni|||0000-0001-8268-4503, Giraldo, Jesús|||0000-0001-7082-4695
Tipo de recurso: artículo
Fecha de publicación:2023
País:España
Institución:Universitat Autònoma de Barcelona
Repositorio:Dipòsit Digital de Documents de la UAB
Idioma:inglés
OAI Identifier:oai:ddd.uab.cat:306801
Acceso en línea:https://ddd.uab.cat/record/306801
https://dx.doi.org/urn:doi:10.1016/j.drudis.2022.103441
Access Level:acceso abierto
Palabra clave:Allosteric modulation
Binding kinetics
Binding cooperativity
Rate constant
Cooperativity rate constant
Residence time
GPCRs
Heterodimer receptor
Descripción
Sumario:Allosteric modulators are of prime interest in drug discovery. These drugs regulate the binding and function of endogenous ligands, with some advantages over orthosteric ligands. A typical pharmacological parameter in allosteric modulation is binding cooperativity. This property can yield unexpected but illuminating results when decomposed into its kinetic parameters. Using two reference models (the allosteric ternary complex receptor model and a heterodimer receptor model), a relationship has been derived for the cooperativity rate constant parameters. This relationship allows many combinations of the cooperativity kinetic parameters for a single binding cooperativity value obtained under equilibrium conditions. This assessment may help understand striking experimental results involving allosteric modulation and suggest further investigations in the field.