| Literature DB >> 18472269 |
Fujie Tanaka1, Yunfeng Hu, Jori Sutton, Lily Asawapornmongkol, Roberta Fuller, Arthur J Olson, Carlos F Barbas, Richard A Lerner.
Abstract
Phage-displayed peptides that selectively bind to aldolase catalytic antibody 93F3 when bound to a particular 1,3-diketone hapten derivative have been developed using designed selection strategies with libraries containing 7-12 randomized amino acid residues. These phage-displayed peptides discriminated the particular 93F3-diketone complex from ligand-free 93F3 and from 93F3 bound to other 1,3-diketone hapten derivatives. By altering the selection procedures, phage-displayed peptides that bind to antibody 93F3 in the absence of 1,3-diketone hapten derivatives have also been developed. With using these phage-displayed peptides, ligand-bound states of the antibody were distinguished from each other. A docking model of one of the peptides bound to the antibody 93F3-diketone complex was created using a sequential divide-and-conquer peptide docking strategy; the model suggests that the peptide interacts with both the antibody and the ligand through a delicate hydrogen bonding network.Entities:
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Year: 2008 PMID: 18472269 PMCID: PMC2452761 DOI: 10.1016/j.bmc.2008.04.062
Source DB: PubMed Journal: Bioorg Med Chem ISSN: 0968-0896 Impact factor: 3.641