Antimicrobial activity of human islet amyloid polypeptides: an insight into amyloid peptides' connection with antimicrobial peptides

Biol Chem. 2012 Jul;393(7):641-6. doi: 10.1515/hsz-2012-0107.

Abstract

Human islet amyloid polypeptide (hIAPP) shows an antimicrobial activity towards two types of clinically relevant bacteria. The potency of hIAPP varies with its aggregation states. Circular dichroism was employed to determine the interaction between hIAPP and bacteria lipid membrane mimic. The antimicrobial activity of each aggregate species is associated with their ability to induce membrane disruption. Our findings provide new evidence revealing the antimicrobial activity of amyloid peptide, which suggest a possible connection between amyloid peptides and antimicrobial peptides.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid beta-Peptides / chemistry
  • Amyloid beta-Peptides / metabolism
  • Amyloid beta-Peptides / pharmacology
  • Anti-Infective Agents / chemistry
  • Anti-Infective Agents / metabolism
  • Anti-Infective Agents / pharmacology*
  • Antimicrobial Cationic Peptides / pharmacology*
  • Cell Membrane / drug effects
  • Cell Membrane / metabolism
  • Escherichia coli / cytology
  • Escherichia coli / drug effects
  • Humans
  • Islet Amyloid Polypeptide / chemistry
  • Islet Amyloid Polypeptide / metabolism
  • Islet Amyloid Polypeptide / pharmacology*
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism
  • Peptide Fragments / pharmacology
  • Protein Multimerization
  • Protein Structure, Secondary
  • Staphylococcus aureus / cytology
  • Staphylococcus aureus / drug effects

Substances

  • Amyloid beta-Peptides
  • Anti-Infective Agents
  • Antimicrobial Cationic Peptides
  • Islet Amyloid Polypeptide
  • Peptide Fragments
  • amyloid beta-protein (1-42)