Factors affecting interactions between sulphonate-terminated dendrimers and proteins: A three case study

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Authors
González García, EstefaníaUniversity of Alcalá Author; Maly, Marek; Mata de la Mata, Francisco Javier de laUniversity of Alcalá Author; Gómez Ramírez, RafaelUniversity of Alcalá Author; Marina Alegre, María LuisaUniversity of Alcalá Author; [et al.]
Identifiers
Permanent link (URI): http://hdl.handle.net/10017/48152
DOI: 10.1016/j.colsurfb.2016.10.020
ISSN: 0927-7765
Date
2017-01-01
Academic Departments
Universidad de Alcalá. Departamento de Química Analítica, Química Física e Ingeniería Química
Universidad de Alcalá. Departamento de Química Orgánica y Química Inorgánica
Teaching unit
Unidad docente Química Analítica e Ingeniería Quimica
Funders
Ministerio de Economía y Empresa
Comunidad de Madrid
Junta de Castilla y León
Bibliographic citation
Colloids and Surfaces B: Biointerfaces, 2017, v. 149, p. 196-205
Keywords
Sulphonate-terminated carbosilane dendrimers
Protein-dendrimer interaction
Fluorescence
Quenching
Computer modeling
Molecular dynamics
Project
info:eu-repo/grantAgreement/GARC//GA13-06989S/ES/Materials engineering towards Innovative Graetzel solar cells
info:eu-repo/grantAgreement/MINECO//AGL2012-36362/ES/VALORIZACION DE RESIDUOS SOLIDOS VEGETALES PROCEDENTES DE LA INDUSTRIA AGROALIMENTARIA
info:eu-repo/grantAgreement/MINECO//CTQ-2014-54004-P/ES/Diseño de sistemas dendríticos avanzados para su uso en biomedicina obtenidos a través de procesos de dendronización
info:eu-repo/grantAgreement/Junta de Castilla y León//S2011%2FBMD-2351/ES/Nanosistemas dendríticos como agentes y vectores terapeúticos en distintas aplicaciones biomédicas
Document type
info:eu-repo/semantics/article
Version
info:eu-repo/semantics/publishedVersion
Rights
Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
© Elsevier
Access rights
info:eu-repo/semantics/openAccess
Abstract
This work proposes a deep study on the interactions between sulphonate-terminated carbosilane dendrimers and proteins. Three different proteins with different molecular weights and isoelectric points were employed and different pHs, dendrimer concentrations and generations were tested. Variations in fluorescence intensity and emission wavelength were used as protein-dendrimer interaction probes. Interaction between dendrimers and proteins greatly depended on the protein itself and pH. Other important issues were the dendrimer concentration and generation. Protein-dendrimer interactions were favored under acidic working conditions when proteins were positively charged. Moreover, in general, high dendrimer generations promoted these interactions. Modeling of protein-dendrimer interactions allowed to understand the different behaviors observed for every protein. (C) 2016 Elsevier B.V. All rights reserved.

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