Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Adsorption of poly(ethylene glycol) amphiphiles to form coatings which inhibit protein adsorption
YKI – Ytkemiska institutet.
1996 (English)In: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 177, p. 502-512Article in journal (Refereed)
Abstract [en]

The adsorption of poly(ethylene glycol) (PEG)-esterified fatty acids at methylated silica, phosphatidic acid and phosphatidylcholine surfaces was investigated with in situ ellipsometry. For a series of PEG-fatty acid esters of ethoxy groups and acyl tails of the type Ci:j-EO151 (16≤i≤18, 0≤j≤2) adsorption at methylated silica was independent of bulk micellization, and plateau was reached below the critical micellization concentration (CMC). The plateau adsorbed amount for the investigated fatty acid esters was only weakly dependent on the nature of the hydrophobic moiety. Instead, saturation adsorption was largely determined by the interactions between PEG chains. Adsorption isotherms were therfore essentially identical on all three of the quite different surfaces. At saturation adsorption, the adsorbed layer thickness was 10-15 nm, while the average adsorbed layer concentration was 0.07 g/cm3. Formation of the PEG-surfactant coatings thus appeared to involve significant molecular alterations of PEG from a random coil. The ability of the PEG-ester coatings to inhibit protein adsorption was also investigated. At adsorption plateau, all coatings investigated displayed quite good ability to inhibit adsorption by a number of serum proteins. For all three surfaces studied this ability decreased below 0.2·CMC. These findings are discussed in relation to the ability of PEG-derivatized lipids to control the in vivo fate of colloidal drug carriers.

Place, publisher, year, edition, pages
1996. Vol. 177, p. 502-512
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:ri:diva-26745OAI: oai:DiVA.org:ri-26745DiVA, id: diva2:1053748
Note
A1030Available from: 2016-12-08 Created: 2016-12-08 Last updated: 2017-11-29Bibliographically approved

Open Access in DiVA

No full text in DiVA

By organisation
YKI – Ytkemiska institutet
In the same journal
Journal of Colloid and Interface Science
Natural Sciences

Search outside of DiVA

GoogleGoogle Scholar

urn-nbn

Altmetric score

urn-nbn
Total: 5 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
v. 2.33.0