TY - JOUR
T1 - Characterization of antimicrobial peptide activity by electrochemical impedance spectroscopy
AU - Chang, William K.
AU - Wimley, William C.
AU - Searson, Peter C.
AU - Hristova, Kalina
AU - Merzlyakov, Mikhail
N1 - Funding Information:
This work was supported by NSF grant MCB 0718841 (KH), NIH grant GM60000 (WCW) and a Louisiana Board of Regents RC/EEP grant (WCW).
PY - 2008/10
Y1 - 2008/10
N2 - Electrochemical impedance spectroscopy performed on surface-supported bilayer membranes allows for the monitoring of changes in membrane properties, such as thickness, ion permeability, and homogeneity, after exposure to antimicrobial peptides (AMPs). We show that two model cationic peptides, very similar in sequence but different in activity, induce dramatically different changes in membrane properties as probed by impedance spectroscopy. Moreover, the impedance results excluded the "barrel-stave" and the "toroidal pore" models of AMP mode of action, and are more consistent with the "carpet" and the "detergent" models. The impedance data provide important new insights about the kinetics and the scale of the peptide action which currently are not addressed by the "carpet" and the "detergent" models. The method presented not only provides additional information about the mode of action of a particular AMP, but offers a means of characterizing AMP activity in reproducible, well-defined quantitative terms.
AB - Electrochemical impedance spectroscopy performed on surface-supported bilayer membranes allows for the monitoring of changes in membrane properties, such as thickness, ion permeability, and homogeneity, after exposure to antimicrobial peptides (AMPs). We show that two model cationic peptides, very similar in sequence but different in activity, induce dramatically different changes in membrane properties as probed by impedance spectroscopy. Moreover, the impedance results excluded the "barrel-stave" and the "toroidal pore" models of AMP mode of action, and are more consistent with the "carpet" and the "detergent" models. The impedance data provide important new insights about the kinetics and the scale of the peptide action which currently are not addressed by the "carpet" and the "detergent" models. The method presented not only provides additional information about the mode of action of a particular AMP, but offers a means of characterizing AMP activity in reproducible, well-defined quantitative terms.
KW - Antimicrobial peptides
KW - Cationic peptides
KW - Electrochemical impedance spectroscopy
KW - Membrane electrochemical properties
KW - Peptide-membrane interaction
KW - Planar supported bilayer
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U2 - 10.1016/j.bbamem.2008.06.016
DO - 10.1016/j.bbamem.2008.06.016
M3 - Article
C2 - 18657512
AN - SCOPUS:52049088052
SN - 0005-2736
VL - 1778
SP - 2430
EP - 2436
JO - Biochimica et Biophysica Acta - Biomembranes
JF - Biochimica et Biophysica Acta - Biomembranes
IS - 10
ER -