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Affilin™ Molecules: Novel Ligands for Bioseparation

Paper ID Volume ID Publish Year Pages File Format Full-Text
19612 43084 2006 6 PDF Available
Title
Affilin™ Molecules: Novel Ligands for Bioseparation
Abstract

With the success of biotherapeutics the need for new ligands for affinity purification is growing. A novel approach to generate customized ligands is the use of alternative binding proteins. Here, we describe the generation, selection, and the use of specific Affilin™ molecules as small and robust ligands for recombinant protein purification. The Affilin™ molecules were isolated from a complex phage display library based on the randomization of eight surface exposed amino acids of the human eye lens protein γ-B-crystallin. Characterization of Affilin™ candidates by surface plasmon resonance (SPR) revealed dissociation constants in the nanomolar range. The E9 Affilin™ variant which was characterized in more detail has nanomolar affinity to the pro-form of human nerve growth factor (proNGF) and was used for matrix coupling to test proNGF recovery. The use of E9 Affilin™ as a ligand in affinity chromatography has demonstrated efficient recovery of its target protein, proNGF, from complex mixtures, such as spiked CHO supernatant or E. coli crude extract. Further, it has been shown that the E9 Affilin™ ligand can withstand denaturing conditions standard for cleaning processes in affinity chromatography. These findings suggest the application of Affilin™ molecules as potent and versatile ligands for affinity chromatography in the field of bioseparation.

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Publisher
Database: Elsevier - ScienceDirect
Journal: Food and Bioproducts Processing - Volume 84, Issue 1, March 2006, Pages 3-8
Authors
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