Simulation studies of the interaction of antimicrobial peptides and lipid bilayers.
Experimental studies of a number of antimicrobial peptides are sufficiently detailed to allow computer simulations to make a significant contribution to understanding their mechanisms of action at an atomic level. In this review we focus on simulation studies of alamethicin, melittin, dermaseptin an...
| Main Authors: | , , , |
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| Format: | Journal article |
| Language: | English |
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1999
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| _version_ | 1826301765130125312 |
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| author | La Rocca, P Biggin, P Tieleman, D Sansom, MS |
| author_facet | La Rocca, P Biggin, P Tieleman, D Sansom, MS |
| author_sort | La Rocca, P |
| collection | OXFORD |
| description | Experimental studies of a number of antimicrobial peptides are sufficiently detailed to allow computer simulations to make a significant contribution to understanding their mechanisms of action at an atomic level. In this review we focus on simulation studies of alamethicin, melittin, dermaseptin and related antimicrobial, membrane-active peptides. All of these peptides form amphipathic alpha-helices. Simulations allow us to explore the interactions of such peptides with lipid bilayers, and to understand the effects of such interactions on the conformational dynamics of the peptides. Mean field methods employ an empirical energy function, such as a simple hydrophobicity potential, to provide an approximation to the membrane. Mean field approaches allow us to predict the optimal orientation of a peptide helix relative to a bilayer. Molecular dynamics simulations that include an atomistic model of the bilayer and surrounding solvent provide a more detailed insight into peptide-bilayer interactions. In the case of alamethicin, all-atom simulations have allowed us to explore several steps along the route from binding to the membrane surface to formation of transbilayer ion channels. For those antimicrobial peptides such as dermaseptin which prefer to remain at the surface of a bilayer, molecular dynamics simulations allow us to explore the favourable interactions between the peptide helix sidechains and the phospholipid headgroups. |
| first_indexed | 2024-03-07T05:37:18Z |
| format | Journal article |
| id | oxford-uuid:e45b92ec-c854-4aeb-a9ee-55159fcd8b8d |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T05:37:18Z |
| publishDate | 1999 |
| record_format | dspace |
| spelling | oxford-uuid:e45b92ec-c854-4aeb-a9ee-55159fcd8b8d2022-03-27T10:15:58ZSimulation studies of the interaction of antimicrobial peptides and lipid bilayers.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:e45b92ec-c854-4aeb-a9ee-55159fcd8b8dEnglishSymplectic Elements at Oxford1999La Rocca, PBiggin, PTieleman, DSansom, MSExperimental studies of a number of antimicrobial peptides are sufficiently detailed to allow computer simulations to make a significant contribution to understanding their mechanisms of action at an atomic level. In this review we focus on simulation studies of alamethicin, melittin, dermaseptin and related antimicrobial, membrane-active peptides. All of these peptides form amphipathic alpha-helices. Simulations allow us to explore the interactions of such peptides with lipid bilayers, and to understand the effects of such interactions on the conformational dynamics of the peptides. Mean field methods employ an empirical energy function, such as a simple hydrophobicity potential, to provide an approximation to the membrane. Mean field approaches allow us to predict the optimal orientation of a peptide helix relative to a bilayer. Molecular dynamics simulations that include an atomistic model of the bilayer and surrounding solvent provide a more detailed insight into peptide-bilayer interactions. In the case of alamethicin, all-atom simulations have allowed us to explore several steps along the route from binding to the membrane surface to formation of transbilayer ion channels. For those antimicrobial peptides such as dermaseptin which prefer to remain at the surface of a bilayer, molecular dynamics simulations allow us to explore the favourable interactions between the peptide helix sidechains and the phospholipid headgroups. |
| spellingShingle | La Rocca, P Biggin, P Tieleman, D Sansom, MS Simulation studies of the interaction of antimicrobial peptides and lipid bilayers. |
| title | Simulation studies of the interaction of antimicrobial peptides and lipid bilayers. |
| title_full | Simulation studies of the interaction of antimicrobial peptides and lipid bilayers. |
| title_fullStr | Simulation studies of the interaction of antimicrobial peptides and lipid bilayers. |
| title_full_unstemmed | Simulation studies of the interaction of antimicrobial peptides and lipid bilayers. |
| title_short | Simulation studies of the interaction of antimicrobial peptides and lipid bilayers. |
| title_sort | simulation studies of the interaction of antimicrobial peptides and lipid bilayers |
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