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Antimicrobial Proteins01:23

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Antimicrobial proteins are important components of the immune system. They aid the body in combating pathogens by either killing them directly or hindering their replication processes. Four main types of antimicrobial substances are interferons, the complement system, iron-binding proteins, and antimicrobial proteins.
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Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
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AI-guided multi-objective optimization identifies a Jelleine I-derived gram-negative antimicrobial peptide lead.

Jun Du1, Xinlu Ren2, Jianna Meng2

  • 1School of Basic Medical Sciences, Lanzhou University, Donggang West Road, Lanzhou, 730000, China; Gansu Provincial Maternity and Child Care Hospital, North Road 143, Qilihe District, Lanzhou, 730000, China.

European Journal of Medicinal Chemistry
|June 25, 2026
PubMed
Summary
This summary is machine-generated.

Researchers used AI to design YB18, a novel antimicrobial peptide. This peptide shows strong antibacterial activity, low toxicity, and forms a hydrogel for wound infections, offering a promising alternative to antibiotics.

Keywords:
Antimicrobial peptideGram-negative bacteriaJelleine IMulti-objective optimizationPeptide hydrogelReinforcement learning

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Area of Science:

  • Biochemistry
  • Computational Biology
  • Materials Science

Background:

  • Antimicrobial peptides (AMPs) offer alternatives to antibiotics but face challenges in optimizing potency, safety, and formulation.
  • Jelleine-I (J1) serves as a scaffold for developing improved AMPs.

Purpose of the Study:

  • To develop an AI-driven framework for multi-objective optimization of AMPs.
  • To identify novel AMPs with enhanced antibacterial activity, mammalian-cell compatibility, and self-assembly properties.

Main Methods:

  • Utilized multi-task learning and reinforcement learning for AMP design.
  • Experimentally validated AI-designed analogues, focusing on YB18.
  • Assessed antibacterial potency, hemolytic activity, cytocompatibility, and mechanism of action.
  • Evaluated in vivo efficacy in an *E. coli*-infected wound model.
  • Characterized self-assembly and hydrogel formation properties.

Main Results:

  • Identified YB18 (RFRLILRL-NH2) as a Gram-negative-directed lead with improved potency (MIC 8-16 µM) over Jelleine-I.
  • YB18 demonstrated low hemolytic activity and good cytocompatibility.
  • Mechanism involves membrane permeability and potential disruption.
  • Topical YB18 reduced bacterial burden in vivo.
  • YB18 formed a viscoelastic hydrogel, further reducing bacterial counts and showing good tolerability in wound models.

Conclusions:

  • YB18 is a promising peptide lead for localized anti-infective applications.
  • AI-guided multi-objective optimization is an effective strategy for AMP discovery and development.