Jonathan W Day, Chan Hyuk Kim, Vaughn V Smider, Peter G Schultz
Department of Chemistry and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Bioorganic & medicinal chemistry letters 2013 May 1The bidentate metal binding amino acid bipyridylalanine (BpyAla) was incorporated into a disulfide linked cyclic peptide phage displayed library to identify metal ion binding peptides. Selection against Ni(2+)-nitrilotriacetic acid (NTA) enriched for sequences containing histidine and BpyAla. BpyAla predominated when selections were carried out at lower pH, consistent with the differential pKa's of histidine and BpyAla. Two peptides containing BpyAla were synthesized and found to bind Ni(2+) with low micromolar dissociation constants. Incorporation of BpyAla and other metal binding amino acids into peptide and protein libraries should enable the evolution of novel binding and catalytic activities. Copyright © 2013. Published by Elsevier Ltd.
Jonathan W Day, Chan Hyuk Kim, Vaughn V Smider, Peter G Schultz. Identification of metal ion binding peptides containing unnatural amino acids by phage display. Bioorganic & medicinal chemistry letters. 2013 May 1;23(9):2598-600
PMID: 23541674
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