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Related Experiment Video

Updated: May 8, 2026

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
08:48

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation

Published on: January 26, 2016

Development and structure-guided characterization of a novel ACE2-binding macrocyclic peptide.

Roger M Benoit1, Jinling Wang2, Darja Beyer3

  • 1Laboratory for Multiscale Bioimaging, PSI Center for Life Sciences, 5232 Villigen PSI, Switzerland.

Journal of Structural Biology: X
|May 7, 2026
PubMed
Summary
This summary is machine-generated.

Researchers discovered WJL-63, a peptide that binds to Angiotensin-converting enzyme 2 (ACE2). This peptide’s unique binding mode and structure enable the development of new ACE2-modulating compounds and imaging agents.

Keywords:
ACE2 structure and conformationMacrocyclic peptidesModulation of ACE2 conformationStructure-based development of imaging agents

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Medicine

Background:

  • Angiotensin-converting enzyme 2 (ACE2) is vital for blood pressure and electrolyte balance within the renin-angiotensin-aldosterone system (RAAS).
  • ACE2 serves as the primary receptor for SARS-CoV and SARS-CoV-2 spike proteins, mediating viral entry.

Purpose of the Study:

  • To identify and characterize novel ACE2-binding molecules.
  • To elucidate the structural basis of peptide-ACE2 interactions.
  • To explore the potential of ACE2-binding peptides for therapeutic and diagnostic applications.

Main Methods:

  • Peptide identification via mRNA display.
  • Biochemical characterization of ACE2-peptide binding.
  • X-ray crystallography to determine the ACE2-WJL-63 complex structure at 2.2 Å resolution.
  • Radiolabeling of WJL-63 with DOTA and evaluation of binding affinity (KD).

Main Results:

  • The macrocyclic peptide WJL-63 was identified and characterized.
  • The crystal structure revealed WJL-63 binds to the ACE2 catalytic cleft in an upright mode, distinct from small-molecule inhibitors.
  • WJL-63 residues Q4, R7, R11, and R14 are crucial for anchoring the peptide.
  • The radiolabeled DOTA-WJL-63 showed a KD of 90 ± 28 nM in binding assays.
  • The binding mode necessitates an open ACE2 conformation.

Conclusions:

  • The ACE2-WJL-63 complex structure provides a blueprint for designing compounds that modulate ACE2 conformation.
  • WJL-63 serves as a scaffold for developing imaging agents for ACE2 visualization.
  • This work opens avenues for developing novel therapeutics and diagnostic tools targeting ACE2.