ISSN:
0947-6539
Keywords:
autocatalysis
;
coiled coil
;
kinetics
;
peptides
;
self-replication
;
Chemistry
;
General Chemistry
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
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.
Additional Material:
11 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/chem.19970030706
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