Abstract
Protegrin 1 (PG-1) is a naturally occurring cationic antimicrobial peptide that is 18 residues long, has an aminated carboxy terminus and contains two disulphide bridges. Here, we investigated the antimicrobial activity of PG-1 and three linear analogues. Then, the membrane permeabilisation induced by these peptides was studied upon Xenopus laevis oocytes by electrophysiological methods. From the results obtained, we concluded that protegrin is able to form anion channels. Moreover, it seems clear that the presence of disulphide bridges is a prerequisite for the pore formation at the membrane level and not for the antimicrobial activity.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
Animals
-
Anti-Bacterial Agents / chemistry
-
Anti-Bacterial Agents / pharmacology
-
Antimicrobial Cationic Peptides
-
Blood Proteins / pharmacology
-
Calcium / metabolism
-
Cell Membrane Permeability / drug effects*
-
Defensins
-
Disulfides / chemistry
-
Disulfides / pharmacology*
-
Escherichia coli / drug effects
-
Ion Channels / drug effects
-
Ion Channels / metabolism
-
Microbial Sensitivity Tests
-
Molecular Sequence Data
-
Oocytes
-
Patch-Clamp Techniques
-
Peptides / chemistry
-
Peptides / pharmacology
-
Proteins / chemistry
-
Proteins / pharmacology*
-
Sequence Alignment
-
Staphylococcus / drug effects
-
Structure-Activity Relationship
-
Xenopus laevis
Substances
-
Anti-Bacterial Agents
-
Antimicrobial Cationic Peptides
-
Blood Proteins
-
Defensins
-
Disulfides
-
Ion Channels
-
Peptides
-
Proteins
-
protegrin-1
-
Calcium