Structure-activity relationship study of the plant-derived decapeptide OSIP108 inhibiting Candida albicans biofilm formation

Antimicrob Agents Chemother. 2014 Aug;58(8):4974-7. doi: 10.1128/AAC.03336-14. Epub 2014 Jun 9.

Abstract

We performed a structure-activity relationship study of the antibiofilm plant-derived decapeptide OSIP108. Introduction of positively charged amino acids R, H, and K resulted in an up-to-5-fold-increased antibiofilm activity against Candida albicans compared to native OSIP108, whereas replacement of R9 resulted in complete abolishment of its antibiofilm activity. By combining the most promising amino acid substitutions, we found that the double-substituted OSIP108 analogue Q6R/G7K had an 8-fold-increased antibiofilm activity.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution
  • Antifungal Agents / chemistry*
  • Antifungal Agents / pharmacology
  • Arabidopsis / chemistry
  • Arabidopsis Proteins / chemistry*
  • Arabidopsis Proteins / pharmacology
  • Arginine / chemistry
  • Biofilms / drug effects*
  • Biofilms / growth & development
  • Candida albicans / drug effects*
  • Candida albicans / physiology
  • Histidine / chemistry
  • Lysine / chemistry
  • Microbial Sensitivity Tests
  • Molecular Sequence Data
  • Static Electricity
  • Structure-Activity Relationship

Substances

  • Antifungal Agents
  • Arabidopsis Proteins
  • methionyl-leucyl-cysteinyl-valyl-leucyl-glutaminyl-glycyl-leucyl-arginyl-glutamic acid
  • Histidine
  • Arginine
  • Lysine