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Related Concept Videos

Lytic Cycle of Bacteriophages01:30

Lytic Cycle of Bacteriophages

Bacteriophages, also known as phages, are specialized viruses that infect bacteria. A key characteristic of phages is their distinctive “head-tail” morphology. A phage begins the infection process (i.e., lytic cycle) by attaching to the outside of a bacterial cell. Attachment is accomplished via proteins in the phage tail that bind to specific receptor proteins on the outer surface of the bacterium. The tail injects the phage’s DNA genome into the bacterial cytoplasm. In the lytic replication...
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Phage-encoded combinatorial chemical libraries based on bicyclic peptides.

Christian Heinis1, Trevor Rutherford, Stephan Freund

  • 1Laboratory of Molecular Biology, Medical Research Council, Cambridge, UK.

Nature Chemical Biology
|June 2, 2009
PubMed
Summary

Researchers developed a phage display method to create novel peptide macrocycles. This strategy successfully generated a potent inhibitor for human plasma kallikrein, impacting blood coagulation.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Drug Discovery

Background:

  • Phage display is a powerful technique for selecting proteins and peptides with specific binding properties.
  • Developing novel macrocyclic peptides as therapeutic agents requires efficient selection and synthesis strategies.

Purpose of the Study:

  • To develop a phage display strategy for generating and selecting bicyclic peptide macrocycles.
  • To identify potent inhibitors of human plasma kallikrein using this novel approach.

Main Methods:

  • Designed peptide repertoires with three reactive cysteine residues fused to phage gene-3-protein.
  • Conjugated peptides with tris-(bromomethyl)benzene to form bicyclic structures anchored to a mesitylene core.
  • Employed iterative affinity selections and mutagenesis for optimization.

Main Results:

  • Generated diverse libraries of bicyclic peptide conjugates.
  • Identified several enzyme inhibitors, including a lead inhibitor (PK15) with high affinity (Ki =1.5 nM) for human plasma kallikrein.
  • Demonstrated that PK15 effectively interrupted the intrinsic coagulation pathway ex vivo.

Conclusions:

  • The described phage strategy is effective for generating and selecting bicyclic macrocycles as ligands.
  • This approach bridges the gap between small-molecule drugs and biologics for therapeutic development.
  • The identified human plasma kallikrein inhibitor has potential therapeutic applications in coagulation disorders.