Peptide–membrane interaction between targeting and lysis
Certain cationic peptides interact with biological membranes. These often-complex interactions can result in peptide targeting to the membrane, or in membrane permeation, rupture, and cell lysis. We investigated the relationship between the structural features of membrane-active peptides and these e...
| Main Authors: | , , , , , , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
American Chemical Society
2017
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| _version_ | 1826312265519857664 |
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| author | Stutz, K Kornmann, B Müller, AT Hiss, JA Schneider, P Blatter, M Pfeiffer, B Posselt, G Kanfer, G Wrede, P Altmann, K-H Wessler, S Schneider, G |
| author_facet | Stutz, K Kornmann, B Müller, AT Hiss, JA Schneider, P Blatter, M Pfeiffer, B Posselt, G Kanfer, G Wrede, P Altmann, K-H Wessler, S Schneider, G |
| author_sort | Stutz, K |
| collection | OXFORD |
| description | Certain cationic peptides interact with biological membranes. These often-complex interactions can result in peptide targeting to the membrane, or in membrane permeation, rupture, and cell lysis. We investigated the relationship between the structural features of membrane-active peptides and these effects, to better understand these processes. To this end, we employed a computational method for morphing a membranolytic antimicrobial peptide into a nonmembranolytic mitochondrial targeting peptide by "directed simulated evolution." The results obtained demonstrate that superficially subtle sequence modifications can strongly affect the peptides' membranolytic and membrane-targeting abilities. Spectroscopic and computational analyses suggest that N- and C-terminal structural flexibility plays a crucial role in determining the mode of peptide-membrane interaction. |
| first_indexed | 2024-03-07T08:24:58Z |
| format | Journal article |
| id | oxford-uuid:9c83beea-2f6d-4e27-a7f1-3a3494785d4b |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T08:24:58Z |
| publishDate | 2017 |
| publisher | American Chemical Society |
| record_format | dspace |
| spelling | oxford-uuid:9c83beea-2f6d-4e27-a7f1-3a3494785d4b2024-02-13T14:47:53ZPeptide–membrane interaction between targeting and lysisJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:9c83beea-2f6d-4e27-a7f1-3a3494785d4bEnglishSymplectic Elements at OxfordAmerican Chemical Society2017Stutz, KKornmann, BMüller, ATHiss, JASchneider, PBlatter, MPfeiffer, BPosselt, GKanfer, GWrede, PAltmann, K-HWessler, SSchneider, GCertain cationic peptides interact with biological membranes. These often-complex interactions can result in peptide targeting to the membrane, or in membrane permeation, rupture, and cell lysis. We investigated the relationship between the structural features of membrane-active peptides and these effects, to better understand these processes. To this end, we employed a computational method for morphing a membranolytic antimicrobial peptide into a nonmembranolytic mitochondrial targeting peptide by "directed simulated evolution." The results obtained demonstrate that superficially subtle sequence modifications can strongly affect the peptides' membranolytic and membrane-targeting abilities. Spectroscopic and computational analyses suggest that N- and C-terminal structural flexibility plays a crucial role in determining the mode of peptide-membrane interaction. |
| spellingShingle | Stutz, K Kornmann, B Müller, AT Hiss, JA Schneider, P Blatter, M Pfeiffer, B Posselt, G Kanfer, G Wrede, P Altmann, K-H Wessler, S Schneider, G Peptide–membrane interaction between targeting and lysis |
| title | Peptide–membrane interaction between targeting and lysis |
| title_full | Peptide–membrane interaction between targeting and lysis |
| title_fullStr | Peptide–membrane interaction between targeting and lysis |
| title_full_unstemmed | Peptide–membrane interaction between targeting and lysis |
| title_short | Peptide–membrane interaction between targeting and lysis |
| title_sort | peptide membrane interaction between targeting and lysis |
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