Amphiphilicity in homopolymer surfaces reduces nonspecific protein adsorption
Amphiphilic homopolymer films have been immobilized onto substrates to study the interactions of these polymers with proteins. X-ray photoelectron spectroscopy (XPS) was utilized to measure the amount of protein adsorption. Amphiphilic homopolymers have been shown to reduce protein adsorption, despi...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 25(2009), 24 vom: 15. Dez., Seite 13795-9 |
|---|---|
| 1. Verfasser: | |
| Weitere Verfasser: | |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2009
|
| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S. Polymers Proteins Surface-Active Agents |
| Zusammenfassung: | Amphiphilic homopolymer films have been immobilized onto substrates to study the interactions of these polymers with proteins. X-ray photoelectron spectroscopy (XPS) was utilized to measure the amount of protein adsorption. Amphiphilic homopolymers have been shown to reduce protein adsorption, despite the high affinity of the hydrophobic or hydrophilic functional groups by themselves toward proteins. This protein-resistant property seems to arise from the unique molecular-scale alternation of incompatible functionalities. The combination of incompatible functionalities with a predefined alternating pattern within a monomer could provide a potential design for nonfouling materials |
|---|---|
| Beschreibung: | Date Completed 22.09.2010 Date Revised 12.03.2024 published: Print Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/la901692a |