Cargando…
Surfactant-free Colloidal Particles with Specific Binding Affinity
[Image: see text] Colloidal particles with specific binding affinity are essential for in vivo and in vitro biosensing, targeted drug delivery, and micrometer-scale self-assembly. Key to these techniques are surface functionalizations that provide high affinities to specific target molecules. For st...
Autores principales: | , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American
Chemical Society
2017
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5618147/ https://www.ncbi.nlm.nih.gov/pubmed/28847149 http://dx.doi.org/10.1021/acs.langmuir.7b02065 |
_version_ | 1783267122407800832 |
---|---|
author | van der Wel, Casper Bossert, Nelli Mank, Quinten J. Winter, Marcel G. T. Heinrich, Doris Kraft, Daniela J. |
author_facet | van der Wel, Casper Bossert, Nelli Mank, Quinten J. Winter, Marcel G. T. Heinrich, Doris Kraft, Daniela J. |
author_sort | van der Wel, Casper |
collection | PubMed |
description | [Image: see text] Colloidal particles with specific binding affinity are essential for in vivo and in vitro biosensing, targeted drug delivery, and micrometer-scale self-assembly. Key to these techniques are surface functionalizations that provide high affinities to specific target molecules. For stabilization in physiological environments, current particle coating methods rely on adsorbed surfactants. However, spontaneous desorption of these surfactants typically has an undesirable influence on lipid membranes. To address this issue and create particles for targeting molecules in lipid membranes, we present here a surfactant-free coating method that combines high binding affinity with stability at physiological conditions. After activating charge-stabilized polystyrene microparticles with EDC/Sulfo-NHS, we first coat the particles with a specific protein and subsequently covalently attach a dense layer of poly(ethyelene) glycol. This polymer layer provides colloidal stability at physiological conditions as well as antiadhesive properties, while the protein coating provides the specific affinity to the targeted molecule. We show that NeutrAvidin-functionalized particles bind specifically to biotinylated membranes and that Concanavalin A-functionalized particles bind specifically to the glycocortex of Dictyostelium discoideum cells. The affinity of the particles changes with protein density, which can be tuned during the coating procedure. The generic and surfactant-free coating method reported here transfers the high affinity and specificity of a protein onto colloidal polystyrene microparticles. |
format | Online Article Text |
id | pubmed-5618147 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | American
Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-56181472017-09-29 Surfactant-free Colloidal Particles with Specific Binding Affinity van der Wel, Casper Bossert, Nelli Mank, Quinten J. Winter, Marcel G. T. Heinrich, Doris Kraft, Daniela J. Langmuir [Image: see text] Colloidal particles with specific binding affinity are essential for in vivo and in vitro biosensing, targeted drug delivery, and micrometer-scale self-assembly. Key to these techniques are surface functionalizations that provide high affinities to specific target molecules. For stabilization in physiological environments, current particle coating methods rely on adsorbed surfactants. However, spontaneous desorption of these surfactants typically has an undesirable influence on lipid membranes. To address this issue and create particles for targeting molecules in lipid membranes, we present here a surfactant-free coating method that combines high binding affinity with stability at physiological conditions. After activating charge-stabilized polystyrene microparticles with EDC/Sulfo-NHS, we first coat the particles with a specific protein and subsequently covalently attach a dense layer of poly(ethyelene) glycol. This polymer layer provides colloidal stability at physiological conditions as well as antiadhesive properties, while the protein coating provides the specific affinity to the targeted molecule. We show that NeutrAvidin-functionalized particles bind specifically to biotinylated membranes and that Concanavalin A-functionalized particles bind specifically to the glycocortex of Dictyostelium discoideum cells. The affinity of the particles changes with protein density, which can be tuned during the coating procedure. The generic and surfactant-free coating method reported here transfers the high affinity and specificity of a protein onto colloidal polystyrene microparticles. American Chemical Society 2017-08-28 2017-09-26 /pmc/articles/PMC5618147/ /pubmed/28847149 http://dx.doi.org/10.1021/acs.langmuir.7b02065 Text en Copyright © 2017 American Chemical Society This is an open access article published under a Creative Commons Non-Commercial No Derivative Works (CC-BY-NC-ND) Attribution License (http://pubs.acs.org/page/policy/authorchoice_ccbyncnd_termsofuse.html) , which permits copying and redistribution of the article, and creation of adaptations, all for non-commercial purposes. |
spellingShingle | van der Wel, Casper Bossert, Nelli Mank, Quinten J. Winter, Marcel G. T. Heinrich, Doris Kraft, Daniela J. Surfactant-free Colloidal Particles with Specific Binding Affinity |
title | Surfactant-free Colloidal Particles with Specific
Binding Affinity |
title_full | Surfactant-free Colloidal Particles with Specific
Binding Affinity |
title_fullStr | Surfactant-free Colloidal Particles with Specific
Binding Affinity |
title_full_unstemmed | Surfactant-free Colloidal Particles with Specific
Binding Affinity |
title_short | Surfactant-free Colloidal Particles with Specific
Binding Affinity |
title_sort | surfactant-free colloidal particles with specific
binding affinity |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5618147/ https://www.ncbi.nlm.nih.gov/pubmed/28847149 http://dx.doi.org/10.1021/acs.langmuir.7b02065 |
work_keys_str_mv | AT vanderwelcasper surfactantfreecolloidalparticleswithspecificbindingaffinity AT bossertnelli surfactantfreecolloidalparticleswithspecificbindingaffinity AT mankquintenj surfactantfreecolloidalparticleswithspecificbindingaffinity AT wintermarcelgt surfactantfreecolloidalparticleswithspecificbindingaffinity AT heinrichdoris surfactantfreecolloidalparticleswithspecificbindingaffinity AT kraftdanielaj surfactantfreecolloidalparticleswithspecificbindingaffinity |