Effect of CM15 on Supported Lipid Bilayer Probed by Atomic Force Microscopy
Antimicrobial peptides are key components of the immune system. These peptides affect the membrane in various ways; some form nano-sized pores, while others only produce minor defects. Since these peptides are increasingly important in developing antimicrobial drugs, understanding the mechanism of t...
| Main Authors: | , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2023-10-01
|
| Series: | Membranes |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2077-0375/13/11/864 |
| _version_ | 1797458472197947392 |
|---|---|
| author | Olivia D. Walsh Leona Choi Krishna P. Sigdel |
| author_facet | Olivia D. Walsh Leona Choi Krishna P. Sigdel |
| author_sort | Olivia D. Walsh |
| collection | DOAJ |
| description | Antimicrobial peptides are key components of the immune system. These peptides affect the membrane in various ways; some form nano-sized pores, while others only produce minor defects. Since these peptides are increasingly important in developing antimicrobial drugs, understanding the mechanism of their interactions with lipid bilayers is critical. Here, using atomic force microscopy (AFM), we investigated the effect of a synthetic hybrid peptide, CM15, on the membrane surface comprising <i>E. coli</i> polar lipid extract. Direct imaging of supported lipid bilayers exposed to various concentrations of the peptide revealed significant membrane remodeling. We found that CM15 interacts with supported lipid bilayers and forms membrane-spanning defects very quickly. It is found that CM15 is capable of remodeling both leaflets of the bilayer. For lower CM15 concentrations, punctate void-like defects were observed, some of which re-sealed themselves as a function of time. However, for CM15 concentrations higher than 5 µM, the defects on the bilayers became so widespread that they disrupted the membrane integrity completely. This work enhances the understanding of CM15 interactions with the bacterial lipid bilayer. |
| first_indexed | 2024-03-09T16:37:35Z |
| format | Article |
| id | doaj.art-d2555c2947744cf1be34fd20db61d42f |
| institution | Directory Open Access Journal |
| issn | 2077-0375 |
| language | English |
| last_indexed | 2024-03-09T16:37:35Z |
| publishDate | 2023-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Membranes |
| spelling | doaj.art-d2555c2947744cf1be34fd20db61d42f2023-11-24T14:55:15ZengMDPI AGMembranes2077-03752023-10-01131186410.3390/membranes13110864Effect of CM15 on Supported Lipid Bilayer Probed by Atomic Force MicroscopyOlivia D. Walsh0Leona Choi1Krishna P. Sigdel2Department of Physics and Astronomy, California State Polytechnic University, Pomona, CA 91768, USADepartment of Physics and Astronomy, California State Polytechnic University, Pomona, CA 91768, USADepartment of Physics and Astronomy, California State Polytechnic University, Pomona, CA 91768, USAAntimicrobial peptides are key components of the immune system. These peptides affect the membrane in various ways; some form nano-sized pores, while others only produce minor defects. Since these peptides are increasingly important in developing antimicrobial drugs, understanding the mechanism of their interactions with lipid bilayers is critical. Here, using atomic force microscopy (AFM), we investigated the effect of a synthetic hybrid peptide, CM15, on the membrane surface comprising <i>E. coli</i> polar lipid extract. Direct imaging of supported lipid bilayers exposed to various concentrations of the peptide revealed significant membrane remodeling. We found that CM15 interacts with supported lipid bilayers and forms membrane-spanning defects very quickly. It is found that CM15 is capable of remodeling both leaflets of the bilayer. For lower CM15 concentrations, punctate void-like defects were observed, some of which re-sealed themselves as a function of time. However, for CM15 concentrations higher than 5 µM, the defects on the bilayers became so widespread that they disrupted the membrane integrity completely. This work enhances the understanding of CM15 interactions with the bacterial lipid bilayer.https://www.mdpi.com/2077-0375/13/11/864atomic force microscopylipid bilayerantimicrobial peptideAMPhybrid peptidescecropin-A |
| spellingShingle | Olivia D. Walsh Leona Choi Krishna P. Sigdel Effect of CM15 on Supported Lipid Bilayer Probed by Atomic Force Microscopy Membranes atomic force microscopy lipid bilayer antimicrobial peptide AMP hybrid peptides cecropin-A |
| title | Effect of CM15 on Supported Lipid Bilayer Probed by Atomic Force Microscopy |
| title_full | Effect of CM15 on Supported Lipid Bilayer Probed by Atomic Force Microscopy |
| title_fullStr | Effect of CM15 on Supported Lipid Bilayer Probed by Atomic Force Microscopy |
| title_full_unstemmed | Effect of CM15 on Supported Lipid Bilayer Probed by Atomic Force Microscopy |
| title_short | Effect of CM15 on Supported Lipid Bilayer Probed by Atomic Force Microscopy |
| title_sort | effect of cm15 on supported lipid bilayer probed by atomic force microscopy |
| topic | atomic force microscopy lipid bilayer antimicrobial peptide AMP hybrid peptides cecropin-A |
| url | https://www.mdpi.com/2077-0375/13/11/864 |
| work_keys_str_mv | AT oliviadwalsh effectofcm15onsupportedlipidbilayerprobedbyatomicforcemicroscopy AT leonachoi effectofcm15onsupportedlipidbilayerprobedbyatomicforcemicroscopy AT krishnapsigdel effectofcm15onsupportedlipidbilayerprobedbyatomicforcemicroscopy |