Dendrimer-Activated Surfaces for High Density and High Activity Protein Chip Applications
Highly functional Si and glass surfaces for protein immobilization have been prepared by a facile activation of native surface silanol groups. Poly(propyleneimine) dendrimers of generations 1−5 were immobilized onto the surface using a facile room-temperature coupling procedure that involved activat...
Saved in:
Published in | Langmuir Vol. 20; no. 15; pp. 6075 - 6079 |
---|---|
Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
United States
American Chemical Society
20.07.2004
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Summary: | Highly functional Si and glass surfaces for protein immobilization have been prepared by a facile activation of native surface silanol groups. Poly(propyleneimine) dendrimers of generations 1−5 were immobilized onto the surface using a facile room-temperature coupling procedure that involved activation of native silanol groups of glass using 1,1‘-carbonyldiimidazole under anhydrous conditions. The dendrimer-coated surfaces were used to immobilize proteins and were characterized with respect to surface loading and activity. A number of different chemical, physical, and biochemical techniques including contact angle measurement, ellipsometry, and fluorescence microscopy were used to characterize the resulting surfaces. Increasing the dendrimer generation past G-3 led to increased surface amine content, immobilized protein concentration, and the activity of immobilized alkaline phosphatase (used as a test system). Very high activity of the immobilized proteins in the case of higher generation (G-4 and G-5) dendrimers led us to conclude that such an approach has true potential for creating highly functional surfaces for protein chip applications. |
---|---|
Bibliography: | istex:D6C375886BCBAC458D313CC19F7BCDA5B8703930 ark:/67375/TPS-Z376J3XP-7 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0743-7463 1520-5827 |
DOI: | 10.1021/la036271f |