Study of Amino ligands fixation to Macroporous supports and their influence on Albumin adsorption
Heterogeneous networks of ethylene glycol dimethacrylate and 2-hydroxyethyl methacrylate [poly(EGDMA-co-HEMA)] were synthesized by suspension polymerization using different EGDMA contents and agitation speeds. The networks were actived with epichlorhydrine (Ech) or 1,4-butanediol diglycidyl ether (B...
| Autores: | , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2009 |
| País: | Argentina |
| Institución: | Consejo Nacional de Investigaciones Científicas y Técnicas |
| Repositorio: | CONICET Digital (CONICET) |
| Idioma: | inglés |
| OAI Identifier: | oai:ri.conicet.gov.ar:11336/24290 |
| Acceso en línea: | http://hdl.handle.net/11336/24290 |
| Access Level: | acceso abierto |
| Palabra clave: | Albumin Adsorption Hema Heterogeneous Polymers Ion Exchanger https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 |
| Sumario: | Heterogeneous networks of ethylene glycol dimethacrylate and 2-hydroxyethyl methacrylate [poly(EGDMA-co-HEMA)] were synthesized by suspension polymerization using different EGDMA contents and agitation speeds. The networks were actived with epichlorhydrine (Ech) or 1,4-butanediol diglycidyl ether (BDGE), and then hexamethylenediamine (HMDA) or ethylenediamine (EDA) were conjugated to the support by coupling reaction. Here, a higher alkyldiamine concentration and temperature, and a longer reaction time led to higher yields. Amino ligands of the support III were used to analyze their adsorption performance of bovine serum albumin (BSA) from the adsorption kinetic. A more external location of HMDA amino ligands into network led to get the maximum adsorption in a time shorter than that with EDA. Due to its bigger size, the HMDA molecule was attached mostly to the network surface between larger pores, which favored a faster protein adsorption. When derivatives containing BDGE were compared, the EDA ligand displayed a BSA retention higher than that with HMDA, because a shorter separation between the ammonium groups along the spacer arm yielded a stronger electrostatic attraction on the protein. Clearly, the balance obtained between the pores system and the reagents molecular structure used in the formation of Ech-HMDA generated the most efficient BSA adsorption. |
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