Phage-Displayed Libraries for the Selection of Optimal Affinity Peptides for Protein Purification Using Ni-Nitrilotriacetic Acid Chromatography |
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| Authors: | Anshuman V. Patwardhan Gaddam Narsa Goud Richard S. Pasquinelli Richard R. Koepsel Mohammad M. Ataai |
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| Affiliation: | (1) Department of Chemical Engineering and the Center for Biotechnology and Bioengineering, University of Pittsburgh, 300 Technology Drive, Pittsburgh, PA, 15219;(2) Department of Microbiology/Biochemistry, Dental School of Medicine, University of Pittsburgh, Pittsburgh, PA, 15261 |
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| Abstract: | A random hexapeptide library, cloned in bacteriophage, was used to select affinity peptides using nickel-nitrilotriacetic acid (Ni-NTA) columns. The screening protocol was successful by isolating peptides sharing common features and, in most cases, common amino acid sequences were isolated (e.g. WHHHPH, AQHHHH). Ni-NTA chromatography of the fusion phage of the selected peptides exhibited a more homogeneous elution behavior (i.e. elution in one peak) than the most commonly used His6peptide (elution in multiple peaks). |
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