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A 32-residue α-helical peptide with a sequence similiar to that of the GCN4 leucine zipper region is shown to catalyze its own formation by accelerating the amide bond formation of a 17-residue peptide, preactivated as a thiobenzyl ester, and a 15-residue peptide with a N-terminal cysteine. The self-replication process displays parabolic growth characteristics as revealed by a detailed kinetic analysis. Control reactions with single-mutant peptides strongly support a mechanism in which a ternary and/or quaternary complex of the product with both peptide fragments act(s) as the catalytically active intermediate(s). Furthermore, these experiments reveal a remarkable sequence selectivity, as evidenced by the loss of autocatalytic activity as a result of a single replacement of leucine or valine residues with an alanine at the recognition interface.
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