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...

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Publié dans:Langmuir : the ACS journal of surfaces and colloids. - 1985. - 20(2004), 15 vom: 20. Juli, Seite 6075-9
Auteur principal: Pathak, Srikant (Auteur)
Autres auteurs: Singh, Anup K, McElhanon, James R, Dentinger, Paul M
Format: Article
Langue:English
Publié: 2004
Accès à la collection:Langmuir : the ACS journal of surfaces and colloids
Sujets:Journal Article Research Support, U.S. Gov't, Non-P.H.S. Dendrimers Imidazoles Immobilized Proteins Polypropylenes Proteins Silanes poly(propyleneimine) silanol plus... 079V3J9O3X N,N-carbonyldiimidazole 63A10X1FSP Alkaline Phosphatase EC 3.1.3.1
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Résumé: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
Description:Date Completed 07.06.2006
Date Revised 24.11.2016
published: Print
Citation Status MEDLINE
ISSN:1520-5827