Feasibility of cationic carbosilane dendrimers for sustainable protein sample preparation
Autores
Marina Alegre, María Luisa; García López, María Concepción; González García, Estefanía; Mata de la Mata, Francisco Javier de la; Sánchez-Nieves Fernández, JavierIdentificadores
Enlace permanente (URI): http://hdl.handle.net/10017/44568DOI: 10.1016/j.colsurfb.2019.110746
ISSN: 0927-7765
Fecha de publicación
2020-02Fecha fin de embargo
2022-03-01Filiación
Universidad de Alcalá. Departamento de Química Analítica, Química Física e Ingeniería Química; Universidad de Alcalá. Departamento de Química Orgánica y Química InorgánicaCita bibliográfica
Colloids and Surfaces B: Biointerfaces, 2020, v. 186, n. 110746, p. 1-8
Palabras clave
Carbosilane dendrimer
Cationic dendrimer
Interaction
Protein enrichment
Protein purification
Proyectos
info:eu-repo/grantAgreement/MINECO//AGL2016-79010-R/ES/DESARROLLO DE METODOS SOSTENIBLES PARA EL APROVECHAMIENTO DE SUBPRODUCTOS DE LA INDUSTRIA ALIMENTARIA CON ELEVADO CONTENIDO PROTEICO
info:eu-repo/grantAgreement/CAM//S2018%2FBAA-4393/ES/ESTRATEGIAS INTEGRADAS PARA LA MEJORA DE LA CALIDAD, LA SEGURIDAD Y LA FUNCIONALIDAD DE LOS ALIMENTOS: HACIA UNA ALIMENTACIÓN SALUDABLE/AVANSECAL-II
info:eu-repo/grantAgreement/CAM//CTQ2017-86224-P/ES/DENDRONIZACIÓN COMO HERRAMIENTA SINTÉTICA DE OBTENCIÓN DE NANOSISTEMAS DENDRÍTICOS ESPECÍFICAMENTE DISEÑADOS PARA SU USO EN APLICACIONES BIOMÉDICAS
Tipo de documento
info:eu-repo/semantics/article
Versión
info:eu-repo/semantics/publishedVersion
Derechos
Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)
© Elsevier
Derechos de acceso
info:eu-repo/semantics/openAccess
Resumen
Protein sample preparation is the bottleneck in the analysis of proteins. The aim of this work is to evaluate the feasibility of carbosilane dendrimers functionalized with cationic groups to make easier this step. Anionic carbosilane dendrimers (sulphonate- and carboxylate-terminated) have already demonstrated their interaction with proteins and their potential in protein sample preparation. In this work, interactions between positively charged carbosilane dendrimers and different model proteins were studied when working under different pH conditions, dendrimer concentrations, and dendrimer generations. Amino- and trimethylammonium-terminated carbosilane dendrimers presented, in some cases, weak interactions with proteins. Unlike them, carbosilane dendrimers with terminal dimethylamino groups could interact, in many cases, with proteins and these interactions were affected by the pH, the dendrimer concentration, and the dendrimer generation. Moreover, dendrimer precipitation was observed at all pHs, although just second and fourth generation (2 G and 4 G) dendrimers resulted in the formation of complexes with proteins. Under experimental conditions promoting dendrimer-protein interactions, 2 G dimethylamino-terminated dendrimers were proposed as an alternative to other methods used in analytical chemistry or analysis in which an organic solvent or a resin are required to enrich/purify proteins in a complex sample.
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