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.
Copyright © 2014, American Society for Microbiology. All Rights Reserved.
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