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Related Concept Videos

Protein Folding01:25

Protein Folding

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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
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Related Experiment Video

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Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
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Optimizing Amphipathic Antimicrobial Peptides via Helical Wheel Rotation.

Hai Bui Thi Phuong1, Nguyen-Thi Phuong2, Le Minh Bui2

  • 1Faculty of Pharmacy, PHENIKAA University, Hanoi, 12116, Vietnam.

Chemmedchem
|September 8, 2025
PubMed
Summary

Researchers optimized antimicrobial peptides (AMPs) using helical wheel rotation. This strategy enhanced antimicrobial and anticancer activity while significantly reducing hemolytic activity, offering a promising approach for therapeutic peptide development.

Keywords:
BP52amphipathic helixantimicrobial peptideshelical wheel rotationstructural optimization

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Area of Science:

  • Biochemistry and Molecular Biology
  • Peptide Science
  • Drug Discovery

Background:

  • Antimicrobial peptides (AMPs) show potential against drug-resistant microbes and cancer.
  • Therapeutic use of AMPs is hindered by hemolytic activity and moderate potency.
  • Optimizing AMPs requires strategies to improve efficacy and safety.

Purpose of the Study:

  • To explore the
  • helical wheel rotation
  • strategy for optimizing amphipathic α-helical AMPs.
  • To assess the impact of this strategy on antimicrobial, anticancer, and hemolytic properties.
  • To develop safer and more potent AMP derivatives for therapeutic applications.

Main Methods:

  • Development of six rotational variants (BP52-A1 to BP52-A6) and two sequence-modified derivatives (BP52-B1, BP52-B2) from a model peptide (BP52).
  • Evaluation of antimicrobial, anticancer, and hemolytic activities of the engineered peptides.
  • Comparative analysis of derivative properties against the parent peptide.

Main Results:

  • Several derivatives, notably BP52-A6, demonstrated enhanced antimicrobial efficacy.
  • BP52-A6 maintained or improved anticancer potency.
  • All engineered derivatives exhibited significantly reduced hemolytic activity compared to BP52.

Conclusions:

  • Helical wheel rotation is an effective and cost-efficient method for peptide engineering.
  • This strategy can fine-tune AMP selectivity and multifunctionality.
  • Optimized AMPs show potential for safer and more effective therapeutic applications.