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Towards oriented assembly of proteins onto magnetic nanoparticles

Paper ID Volume ID Publish Year Pages File Format Full-Text
4563 232 2008 7 PDF Available
Title
Towards oriented assembly of proteins onto magnetic nanoparticles
Abstract

Magnetic particles, functionalized with transition metal ions, possess the ability to specifically bind recombinant proteins engineered to contain C- or N-terminal histidine residues (e.g., a hexahistidine tag). We have surface-functionalized these particles and developed a simple orientational model that predicts the spatial arrangement of a model histidine tagged protein, green fluorescent protein (GFP), adsorbed to the surface of Fe3O4 magnetite nanoparticle agglomerates. A Langmuir isotherm model can describe well the specific, monolayer adsorption onto the particle surface, and the maximum adsorption capacity was 0.865 μg-GFP/μg particle. We have also determined the net available surface area of these nanoparticles (97 m2/g) and our results suggest a vertical alignment of 88 GFP molecules in a nearly closest packed configuration per “average” nanoparticle. This approach may be useful for characterizing the assembly of other proteins with known shape onto magnetic nanoparticles.

Keywords
Adsorption; Affinity; Bioseparation; Immobilized Enzymes; Magnetic Nanoparticles; Protein Purification
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biochemical Engineering Journal - Volume 38, Issue 2, 15 February 2008, Pages 164–170
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us