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Peptide Self‐Replication Via Template‐Directed Ligation
Author(s) -
Severin Kay,
Lee David H.,
Martinez Jose A.,
Ghadiri M. Reza
Publication year - 1997
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.19970030706
Subject(s) - peptide , cysteine , residue (chemistry) , chemistry , autocatalysis , alanine , stereochemistry , leucine zipper , peptide bond , leucine , valine , peptide sequence , biochemistry , amino acid , catalysis , enzyme , gene
Abstract 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.