Overlapping properties of the short membrane-active peptide BP100 with (i) Polycationic TAT and (ii) α-helical Magainin Family Peptides
| Autor(a) principal: | |
|---|---|
| Data de Publicação: | 2021 |
| Outros Autores: | , , , , , , |
| Tipo de documento: | Artigo |
| Idioma: | eng |
| Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
| Texto Completo: | http://hdl.handle.net/10451/48022 |
Resumo: | Copyright © 2021 Mink, Strandberg, Wadhwani, Melo, Reichert, Wacker, Castanho and Ulrich. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
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Overlapping properties of the short membrane-active peptide BP100 with (i) Polycationic TAT and (ii) α-helical Magainin Family PeptidesShort multifunctional peptide BP100Cationic amphipathic a-helixMembranolytic and cell-penetrating mechanismsAntimicrobial activityHemolysisVesicle fusionVesicle leakageCopyright © 2021 Mink, Strandberg, Wadhwani, Melo, Reichert, Wacker, Castanho and Ulrich. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.BP100 is a short, designer-made membrane-active peptide with multiple functionalities: antimicrobial, cell-penetrating, and fusogenic. Consisting of five lysines and 6 hydrophobic residues, BP100 was shown to bind to lipid bilayers as an amphipathic a-helix, but its mechanism of action remains unclear. With these features, BP100 embodies the characteristics of two distinctly different classes of membrane-active peptides, which have been studied in detail and where the mechanism of action is better understood. On the one hand, its amphiphilic helical structure is similar to the pore forming magainin family of antimicrobial peptides, though BP100 is much too short to span the membrane. On the other hand, its length and high charge density are reminiscent of the HIV-TAT family of cell penetrating peptides, for which inverted micelles have been postulated as translocation intermediates, amongst other mechanisms. Assays were performed to test the antimicrobial and hemolytic activity, the induced leakage and fusion of lipid vesicles, and cell uptake. From these results the functional profiles of BP100, HIV-TAT, and the magainin-like peptides magainin 2, PGLa, MSI-103, and MAP were determined and compared. It is observed that the activity of BP100 resembles most closely the much longer amphipathic a-helical magainin-like peptides, with high antimicrobial activity along with considerable fusogenic and hemolytic effects. In contrast, HIV-TAT shows almost no antimicrobial, fusogenic, or hemolytic effects. We conclude that the amphipathic helix of BP100 has a similar membranebased activity as magainin-like peptides and may have a similar mechanism of action.This work was supported financially by the BIF-TM program of the Helmholtz-Gemeinschaft; by the DFG grant INST 121384/58-1 FUGG; and by the DAAD “Portugal - Acções Integradas Luso-Alemãs/DAAD-GRIC” grant D/07/13644.FrontiersRepositório da Universidade de LisboaMink, ChristianStrandberg, ErikWadhwani, ParveshMelo, Manuel N.Reichert, JohannesWacker, IreneCastanho, Miguel A. R. B.Ulrich, Anne S.2021-05-19T15:10:28Z20212021-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10451/48022engFront Cell Infect Microbiol. 2021 Apr 26;11:60954210.3389/fcimb.2021.6095422235-2988info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-11-08T16:51:12Zoai:repositorio.ul.pt:10451/48022Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T21:59:57.305216Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
| dc.title.none.fl_str_mv |
Overlapping properties of the short membrane-active peptide BP100 with (i) Polycationic TAT and (ii) α-helical Magainin Family Peptides |
| title |
Overlapping properties of the short membrane-active peptide BP100 with (i) Polycationic TAT and (ii) α-helical Magainin Family Peptides |
| spellingShingle |
Overlapping properties of the short membrane-active peptide BP100 with (i) Polycationic TAT and (ii) α-helical Magainin Family Peptides Mink, Christian Short multifunctional peptide BP100 Cationic amphipathic a-helix Membranolytic and cell-penetrating mechanisms Antimicrobial activity Hemolysis Vesicle fusion Vesicle leakage |
| title_short |
Overlapping properties of the short membrane-active peptide BP100 with (i) Polycationic TAT and (ii) α-helical Magainin Family Peptides |
| title_full |
Overlapping properties of the short membrane-active peptide BP100 with (i) Polycationic TAT and (ii) α-helical Magainin Family Peptides |
| title_fullStr |
Overlapping properties of the short membrane-active peptide BP100 with (i) Polycationic TAT and (ii) α-helical Magainin Family Peptides |
| title_full_unstemmed |
Overlapping properties of the short membrane-active peptide BP100 with (i) Polycationic TAT and (ii) α-helical Magainin Family Peptides |
| title_sort |
Overlapping properties of the short membrane-active peptide BP100 with (i) Polycationic TAT and (ii) α-helical Magainin Family Peptides |
| author |
Mink, Christian |
| author_facet |
Mink, Christian Strandberg, Erik Wadhwani, Parvesh Melo, Manuel N. Reichert, Johannes Wacker, Irene Castanho, Miguel A. R. B. Ulrich, Anne S. |
| author_role |
author |
| author2 |
Strandberg, Erik Wadhwani, Parvesh Melo, Manuel N. Reichert, Johannes Wacker, Irene Castanho, Miguel A. R. B. Ulrich, Anne S. |
| author2_role |
author author author author author author author |
| dc.contributor.none.fl_str_mv |
Repositório da Universidade de Lisboa |
| dc.contributor.author.fl_str_mv |
Mink, Christian Strandberg, Erik Wadhwani, Parvesh Melo, Manuel N. Reichert, Johannes Wacker, Irene Castanho, Miguel A. R. B. Ulrich, Anne S. |
| dc.subject.por.fl_str_mv |
Short multifunctional peptide BP100 Cationic amphipathic a-helix Membranolytic and cell-penetrating mechanisms Antimicrobial activity Hemolysis Vesicle fusion Vesicle leakage |
| topic |
Short multifunctional peptide BP100 Cationic amphipathic a-helix Membranolytic and cell-penetrating mechanisms Antimicrobial activity Hemolysis Vesicle fusion Vesicle leakage |
| description |
Copyright © 2021 Mink, Strandberg, Wadhwani, Melo, Reichert, Wacker, Castanho and Ulrich. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
| publishDate |
2021 |
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2021-05-19T15:10:28Z 2021 2021-01-01T00:00:00Z |
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info:eu-repo/semantics/publishedVersion |
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info:eu-repo/semantics/article |
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article |
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publishedVersion |
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http://hdl.handle.net/10451/48022 |
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http://hdl.handle.net/10451/48022 |
| dc.language.iso.fl_str_mv |
eng |
| language |
eng |
| dc.relation.none.fl_str_mv |
Front Cell Infect Microbiol. 2021 Apr 26;11:609542 10.3389/fcimb.2021.609542 2235-2988 |
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info:eu-repo/semantics/openAccess |
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openAccess |
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application/pdf |
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Frontiers |
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Frontiers |
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reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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