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Controlled presentation of recombinant proteins via a zinc-binding peptide-linker in two and three dimensional formats

Paper ID Volume ID Publish Year Pages File Format Full-Text
10097 664 2009 7 PDF Available
Title
Controlled presentation of recombinant proteins via a zinc-binding peptide-linker in two and three dimensional formats
Abstract

The presentation of proteins on surfaces is fundamental to numerous cell culture and tissue engineering applications. While a number of physisorption and cross-linking methods exist to facilitate this process, few avoid denaturation of proteins or allow control over protein orientation, both of which are critical to the functionality of many signal proteins and ligands. Often recombinant protein sequences include a poly-histidine tag to facilitate purification. We utilize this sequence to anchor proteins to biosurfaces via a peptide bonded to the surface which conjugates with the poly-histidine tag in the presence of zinc rather than nickel, which is more traditionally used to conjugate poly-histidine tags to surfaces. We demonstrate that this strategy enables the display of proteins on 2D and 3D surfaces without compromising protein function through direct cross-linking or physisorption.

Keywords
Growth factors; Surface modification; Cell culture; Recombinant protein
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Controlled presentation of recombinant proteins via a zinc-binding peptide-linker in two and three dimensional formats
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biomaterials - Volume 30, Issue 34, December 2009, Pages 6614–6620
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