A small protein was self-assembled on a template. A metal-binding ligand, 4,4'-dicarboxylic acid-2,2'-bipyridine, was attached to the N-terminus of an oligopeptide with the potential to form an amphiphilic alpha -helix. These bipyridine-modified peptides trimerized to form a three alpha -helix bundle protein in the presence of FE(II). The cumulative binding constant was determined to be >5*10 17 M -3 , approximately 25 times greater than that of a control compound with no peptide moiety. Aldehyde templates are being developed to assemble unsymmetrical three alpha -helix bundle proteins.
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Lieberman et al. (1991) studied this question.
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