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Cu2+ reduces hemolytic activity of the antimicrobial peptide HMPI and enhances its trypsin resistance

Jinxiu Peng1, Yang Yang2, Ping Zhao1

  • 1Key Laboratory of Preclinical Study for New Drugs of Gansu Province, Institute of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Lanzhou University, Lanzhou 730000, China.

Acta Biochimica Et Biophysica Sinica
|May 6, 2020
PubMed

Insights

Copper ions (Cu2+) enhance the stability and antifungal activity of antimicrobial peptides (AMPs) like HMPI. This inorganic strategy improves protease resistance and reduces hemolytic activity, offering a promising alternative to conventional antibiotics against drug-resistant microbes.

Area of Science:

  • Microbiology
  • Biochemistry
  • Drug Discovery

Background:

  • Drug-resistant microbes pose a significant global health threat.
  • Antimicrobial peptides (AMPs) show promise as alternatives to conventional antibiotics.
  • AMPs often face limitations due to protease susceptibility and hemolytic activity.

Purpose of the Study:

  • To investigate the effect of Cu2+ on the bioactivity and stability of the antimicrobial peptide HMPI.
  • To explore Cu2+ as a strategy to overcome AMP limitations for clinical applications.

Main Methods:

  • Treatment of AMP HMPI with Cu2+.
  • Assessment of protease resistance, bioactivity, and hemolytic activity.
  • Measurement of reactive oxygen species (ROS) production in fungal cells.

Main Results:

  • Cu2+ addition improved the protease resistance of AMP HMPI without compromising its bioactivity.
  • Binding of Cu2+ significantly decreased the hemolytic activity of HMPI.
  • Cu2+ increased ROS production in fungal cells, potentially enhancing antifungal effects.

Conclusions:

  • Cu2+ can serve as an inorganic strategy to enhance AMP HMPI stability and reduce hemolytic activity.
  • This approach maintains the antifungal efficacy of AMP HMPI, addressing key limitations for therapeutic use.
Keywords:
antifungal activityantimicrobial peptide HMPIproteasestabilitytrypsin

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