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Differentiating antimicrobial peptides interacting with lipid bilayer: Molecular signatures derived from quartz crystal microbalance with dissipation monitoring.
- Source :
-
Biophysical chemistry [Biophys Chem] 2015 Jan; Vol. 196, pp. 53-67. Date of Electronic Publication: 2014 Sep 28. - Publication Year :
- 2015
-
Abstract
- Many antimicrobial peptides (AMPs) kill bacteria by disrupting the lipid bilayer structure of their inner membrane. However, there is only limited quantitative information in the literature to differentiate between AMPs of differing molecular properties, in terms of how they interact with the membrane. In this study, we have used quartz crystal microbalance with dissipation monitoring (QCM-D) to probe the interactions between a supported bilayer membrane of egg phosphatidylcholine (egg PC) and four structurally different AMPs: alamethicin, chrysophsin-3, indolicidin, and sheep myeloid antimicrobial peptide (SMAP-29). Multiple signatures from the QCM-D measurements were extracted, differentiating the AMPs, that provide information on peptide addition to and lipid removal from the membrane, the dynamics of peptide-membrane interactions and the rates at which the peptide actions are initiated. The mechanistic variations in peptide action were related to the fundamental structural properties of the peptides including the hydrophobicity, hydrophobic moment, and the probability of α-helical secondary structures.<br /> (Published by Elsevier B.V.)
- Subjects :
- Alamethicin chemistry
Alamethicin metabolism
Amino Acid Sequence
Animals
Antimicrobial Cationic Peptides chemistry
Blood Proteins chemistry
Blood Proteins metabolism
Cathelicidins chemistry
Cathelicidins metabolism
Hydrophobic and Hydrophilic Interactions
Kinetics
Lipid Bilayers chemistry
Molecular Sequence Data
Phosphatidylcholines chemistry
Protein Structure, Secondary
Sheep
Antimicrobial Cationic Peptides metabolism
Lipid Bilayers metabolism
Quartz Crystal Microbalance Techniques
Subjects
Details
- Language :
- English
- ISSN :
- 1873-4200
- Volume :
- 196
- Database :
- MEDLINE
- Journal :
- Biophysical chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 25307196
- Full Text :
- https://doi.org/10.1016/j.bpc.2014.09.003