A self-replicating peptide

Article Abstract:

A 32-residue alpha-helix peptide, is based on the yeast transcription factor GCN4 leucine-zipper domain, is capable of autocatalysis and self-replication. The peptide catalyzes its own synthesis in neutral, dilute aqueous solutions by accelerating the thioester-promoted amide-bond condensation of 15- and 17-residue fragments. The peptide's self-replication process exhibits parabolic growth, where the initial rate of product formation correlates with the square-root of initial concentration of the template.

Analysis, Peptide synthesis, Catalysis, Autopoiesis

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A synthetic peptide ligase

Article Abstract:

A 33-residue synthetic peptide based on the coiled-coil structural motif has been shown to efficiently catalyze the condensation of two shorter peptide fragments with high sequence- and diastereoselectivity. The high sequence- and diastereoselectivity of the 33-residue ligase was indicated by experiments with altered electrophilic and nucleophilic peptide fragments. This research highlights the use of alpha-helical protein-like assemblies in artificial enzyme design.

Peptide regulatory factors, Ligases

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Antibacterial agents based on the cyclic D,L-alpha-peptide architecture

Article Abstract:

It has been established that six- and eight-residue cyclic D,L-alpha-peptides function preferentially on Gram-positive and/or Gram-negative bacterial membranes compared to mammalian cells. It is suggested that appropriately designed cyclic D,L-alpha-peptides may be capable of selectively targeting and self assembling in bacterial membranes.

Antibacterial agents

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