Autor según el artículo: Orlandini M; Pedrini A; Marchetti D; Li Y; Aragay G; Dalcanale E; Ballester P; Pinalli R
Departamento: Química Analítica i Química Orgànica
Autor/es de la URV: Li, Yifan
Palabras clave: Tetra-aryl-extended calix[4]pyrrole Solvation/desolvation effects Selectivity Post translational modifications Peptides Molecular recognition Methylation Complexation Acetyl lysine
Resumen: Post-translational modifications of lysine in histones, as methylation and acetylation, have well established functions in epigenetics and are emerging as important actors in broader biological regulation. Currently, the detection of acetylated lysine (Kac) in water solution as free amino acid or protein residue remains challenging. Acetylated lysine is a neutral amino acid, and the lack of ion-dipole interactions causes the decrease in binding affinity displayed by synthetic molecular receptors with respect to the other lysine modifications. Here, we report molecular modeling calculations and 1H NMR experiments to investigate the binding properties of two different calix[4]pyrrole receptors towards Kac. Computational analyses reveal that tetra-aryl-extended calix[4]pyrrole (1) preferentially binds the cis-Kac conformer over the trans one due to steric considerations and more favorable interactions. Experimental 1H NMR titration experiments confirm the formation of a 1 : 1 complex between receptor 1 and cis-Kac, with a Ka exceeding 103 M-1. Conversely, the super-aryl-extended calix[4]pyrrole 2 is less efficient in binding Kac, due to unfavorable solvation/desolvation effects, as proven by 1H NMR experiments. Moreover, receptor 1 showed a higher affinity for Kac over other lysine modifications, such as methylated lysines.The selective molecular recognition properties of two different calix[4]pyrrole receptors toward the cis isomer of acetylated lysine (cis-Kac) are investigated. The formation of a 1 : 1 complex is favoured for the aryl-extended receptor compared to the superaryl-extended featuring a deeper cavity for which the energetically not favourable desolvation of the aminoacidic group hampers the guest inclusion in the hydrophobic cavity. image
Áreas temáticas: Química Organic chemistry Medicina i Materiais Interdisciplinar General medicine General chemistry Farmacia Engenharias iii Engenharias ii Ciências biológicas iii Ciências biológicas ii Ciências biológicas i Ciências agrárias i Chemistry, multidisciplinary Chemistry (miscellaneous) Chemistry (all) Chemistry Catalysis Biotecnología Biodiversidade Astronomia / física
Acceso a la licencia de uso: https://creativecommons.org/licenses/by/3.0/es/
Direcció de correo del autor: yifan.li@estudiants.urv.cat
Identificador del autor: 0000-0001-8708-0004
Fecha de alta del registro: 2024-04-06
Versión del articulo depositado: info:eu-repo/semantics/publishedVersion
Enlace a la fuente original: https://chemistry-europe.onlinelibrary.wiley.com/doi/full/10.1002/chem.202303715
URL Documento de licencia: http://repositori.urv.cat/ca/proteccio-de-dades/
Referencia al articulo segun fuente origial: Chemistry-A European Journal. 30 (18): e202303715-e202303715
Referencia de l'ítem segons les normes APA: Orlandini M; Pedrini A; Marchetti D; Li Y; Aragay G; Dalcanale E; Ballester P; Pinalli R (2024). Binding of Acetylated Lysine by Using a Water Soluble Aryl Extended Calix[4]pyrrole. Chemistry-A European Journal, 30(18), e202303715-e202303715. DOI: 10.1002/chem.202303715
DOI del artículo: 10.1002/chem.202303715
Entidad: Universitat Rovira i Virgili
Año de publicación de la revista: 2024
Tipo de publicación: Journal Publications
Repositori URV