Biomembrane interactions reveal the mechanism of action of surface-immobilized host defense IDR-1010 peptide

Guangzheng Gao, John T.J. Cheng, Jason Kindrachuk, Robert Hancock, Suzana K. Straus, Jayachandran N. Kizhakkedathu

Research output: Contribution to journalArticle

31 Citations (Scopus)


Dissecting the mechanism of action of surface-tethered antimicrobial and immunomodulatory peptides is critical to the design of optimized anti-infection coatings on biomedical devices. To address this, we compared the biomembrane interactions of host defense peptide IDR-1010cys (1) in free form, (2) as a soluble polymer conjugate, and (3) with one end tethered to a solid support with model bacterial and mammalian lipid membranes. Our results show that IDR-1010cys in all three distinct forms interacted with bacterial and mammalian lipid vesicles, but the extent of the interactions as monitored by the induction of secondary structure varied. The enhanced interaction of surface-tethered peptides is well correlated with their very good antimicrobial activities. Our results demonstrate that there may be a difference in the mechanism of action of surface-tethered versus free IDR-1010cys.

Original languageEnglish
Pages (from-to)199-209
Number of pages11
JournalChemistry and Biology
Issue number2
Publication statusPublished - 24 Feb 2012
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Clinical Biochemistry

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