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Adsorption of diblock copolymers of poly(ethylene oxide) and poly(lactide) at hydrophobized silica from aqueous solution
YKI – Ytkemiska institutet.
2000 (English)In: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 228, 326-334 p.Article in journal (Refereed)
Abstract [en]

The adsorption of a series of amphiphilic diblock copolymers of poly(ethylene oxide) (PEO) and poly(DL-lactide) (PL) at hydrophobized silica from aqueous solution was studied using time-resolved ellipsometry and reflectometry. The adsorbed amounts only display a weak dependence on the copolymer composition in both water and phosphate-buffered solution. For the short copolymers, the layer thickness decreases slightly with increasing length of the hydrophobic block. Furthermore, in comparison with the short copolymers, the layer thickness of the long copolymers is substantially higher. Upon degradation of the PL block, the adsorbed amount is found to decrease and approach that of the corresponding PEO homopolymer. Protein rejection studies indicate that the adsorption of fibrinogen is inhibited by copolymer preadsorption. The protein rejection is enhanced with increasing surface coverage of the preadsorbed copolymer, but largely independent of the length of the PL block and the PEO block. For all polymers investigated, essentially complete protein rejection is obtained above a critical surface coverage that is significantly lower than the saturation coverage of the copolymers. Removing the copolymer from bulk solution after preadsorption causes a partial desorption, resulting in reduced protein rejection. However, the protein rejection capacity with and without copolymer in the bulk solution is found to be similar at a given surface coverage. Contrary to the behavior of the intact copolymers, fibrinogen adsorption is found to be significant at surfaces pretreated with an extensively degraded copolymer and, in fact, quantitatively comparable to that at the hydrophobic surface in the absence of preadsorption. This finding, together with that of the effect of the copolymer composition on protein rejection, suggests that an efficient protein rejection is maintained until only a few L units remain in the copolymer, i.e., until nearly completed degradation.

Place, publisher, year, edition, pages
2000. Vol. 228, 326-334 p.
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:ri:diva-26715OAI: oai:DiVA.org:ri-26715DiVA: diva2:1053718
Note
A1389Available from: 2016-12-08 Created: 2016-12-08Bibliographically approved

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