The antimicrobial peptide Polybia-MP1 differentiates membranes with the hopanoid, diplopterol from those with cholesterol

Detalhes bibliográficos
Autor(a) principal: Alvares, Dayane S. [UNESP]
Data de Publicação: 2021
Outros Autores: Monti, Mariela R., Ruggiero Neto, João [UNESP], Wilke, Natalia
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1016/j.bbadva.2021.100002
http://hdl.handle.net/11449/228932
Resumo: Polybia-MP1 is an antimicrobial peptide that shows a decreased activity in membranes with cholesterol (CHO). Since it is now accepted that hopanoids act as sterol-surrogates in some sterol-lacking bacteria, we here inquire about the impact of Polybia-MP1 on membranes containing the hopanoid diplopterol (DP) in comparison to membranes with CHO. We found that, despite the properties induced on lipid membranes by DP are similar to those induced by CHO, the effect of Polybia-MP1 on membranes with CHO or DP was significantly different. DP did not prevent dye release from LUVs, nor the insertion of Polybia-MP1 into monolayers, and peptide-membrane affinity was higher for those with DP than with CHO. Zeta potentials (ζ) for DP-containing LUVs showed a complex behavior at increasing peptide concentration. The effect of the peptide on membrane elasticity, investigated by nanotube retraction experiments, showed that peptide addition softened all membrane compositions, but membranes with DP got stiffer at long times. Considering this, and the ζ results, we propose that peptides accumulate at the interface adopting different arrangements, leading to a non-monotonic behavior. Possible correlations with cell membranes were inquired testing the antimicrobial activity of Polybia-MP1 against hopanoid-lacking bacteria pre-incubated with DP or CHO. The fraction of surviving cells was lower in cultures incubated with DP compared to those incubated with CHO. We propose that the higher activity of Polybia-MP1 against some bacteria compared to mammalian cells is not only related to membrane electrostatics, but also the composition of neutral lipids, particularly the hopanoids, could be important.
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spelling The antimicrobial peptide Polybia-MP1 differentiates membranes with the hopanoid, diplopterol from those with cholesterolBacterial resistanceLytic activityMembrane dynamic elasticityOptical tweezersTargeting of AMPsZeta potentialPolybia-MP1 is an antimicrobial peptide that shows a decreased activity in membranes with cholesterol (CHO). Since it is now accepted that hopanoids act as sterol-surrogates in some sterol-lacking bacteria, we here inquire about the impact of Polybia-MP1 on membranes containing the hopanoid diplopterol (DP) in comparison to membranes with CHO. We found that, despite the properties induced on lipid membranes by DP are similar to those induced by CHO, the effect of Polybia-MP1 on membranes with CHO or DP was significantly different. DP did not prevent dye release from LUVs, nor the insertion of Polybia-MP1 into monolayers, and peptide-membrane affinity was higher for those with DP than with CHO. Zeta potentials (ζ) for DP-containing LUVs showed a complex behavior at increasing peptide concentration. The effect of the peptide on membrane elasticity, investigated by nanotube retraction experiments, showed that peptide addition softened all membrane compositions, but membranes with DP got stiffer at long times. Considering this, and the ζ results, we propose that peptides accumulate at the interface adopting different arrangements, leading to a non-monotonic behavior. Possible correlations with cell membranes were inquired testing the antimicrobial activity of Polybia-MP1 against hopanoid-lacking bacteria pre-incubated with DP or CHO. The fraction of surviving cells was lower in cultures incubated with DP compared to those incubated with CHO. We propose that the higher activity of Polybia-MP1 against some bacteria compared to mammalian cells is not only related to membrane electrostatics, but also the composition of neutral lipids, particularly the hopanoids, could be important.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)UNESP - Sao Paulo State University IBILCE Department of PhysicsUniversidad Nacional de Córdoba Facultad de Ciencias Químicas Departamento de Química Biológica Ranwel CaputtoCONICET Universidad Nacional de Córdoba Centro de Investigaciones en Química Biológica de Córdoba (CIQUIBIC)UNESP - Sao Paulo State University IBILCE Department of PhysicsFAPESP: #2015/25619-9Universidade Estadual Paulista (UNESP)Facultad de Ciencias QuímicasCentro de Investigaciones en Química Biológica de Córdoba (CIQUIBIC)Alvares, Dayane S. [UNESP]Monti, Mariela R.Ruggiero Neto, João [UNESP]Wilke, Natalia2022-04-29T08:29:28Z2022-04-29T08:29:28Z2021-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1016/j.bbadva.2021.100002BBA Advances, v. 1.2667-1603http://hdl.handle.net/11449/22893210.1016/j.bbadva.2021.1000022-s2.0-85104980420Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengBBA Advancesinfo:eu-repo/semantics/openAccess2022-04-29T08:29:28Zoai:repositorio.unesp.br:11449/228932Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-06T00:03:54.251433Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv The antimicrobial peptide Polybia-MP1 differentiates membranes with the hopanoid, diplopterol from those with cholesterol
title The antimicrobial peptide Polybia-MP1 differentiates membranes with the hopanoid, diplopterol from those with cholesterol
spellingShingle The antimicrobial peptide Polybia-MP1 differentiates membranes with the hopanoid, diplopterol from those with cholesterol
Alvares, Dayane S. [UNESP]
Bacterial resistance
Lytic activity
Membrane dynamic elasticity
Optical tweezers
Targeting of AMPs
Zeta potential
title_short The antimicrobial peptide Polybia-MP1 differentiates membranes with the hopanoid, diplopterol from those with cholesterol
title_full The antimicrobial peptide Polybia-MP1 differentiates membranes with the hopanoid, diplopterol from those with cholesterol
title_fullStr The antimicrobial peptide Polybia-MP1 differentiates membranes with the hopanoid, diplopterol from those with cholesterol
title_full_unstemmed The antimicrobial peptide Polybia-MP1 differentiates membranes with the hopanoid, diplopterol from those with cholesterol
title_sort The antimicrobial peptide Polybia-MP1 differentiates membranes with the hopanoid, diplopterol from those with cholesterol
author Alvares, Dayane S. [UNESP]
author_facet Alvares, Dayane S. [UNESP]
Monti, Mariela R.
Ruggiero Neto, João [UNESP]
Wilke, Natalia
author_role author
author2 Monti, Mariela R.
Ruggiero Neto, João [UNESP]
Wilke, Natalia
author2_role author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (UNESP)
Facultad de Ciencias Químicas
Centro de Investigaciones en Química Biológica de Córdoba (CIQUIBIC)
dc.contributor.author.fl_str_mv Alvares, Dayane S. [UNESP]
Monti, Mariela R.
Ruggiero Neto, João [UNESP]
Wilke, Natalia
dc.subject.por.fl_str_mv Bacterial resistance
Lytic activity
Membrane dynamic elasticity
Optical tweezers
Targeting of AMPs
Zeta potential
topic Bacterial resistance
Lytic activity
Membrane dynamic elasticity
Optical tweezers
Targeting of AMPs
Zeta potential
description Polybia-MP1 is an antimicrobial peptide that shows a decreased activity in membranes with cholesterol (CHO). Since it is now accepted that hopanoids act as sterol-surrogates in some sterol-lacking bacteria, we here inquire about the impact of Polybia-MP1 on membranes containing the hopanoid diplopterol (DP) in comparison to membranes with CHO. We found that, despite the properties induced on lipid membranes by DP are similar to those induced by CHO, the effect of Polybia-MP1 on membranes with CHO or DP was significantly different. DP did not prevent dye release from LUVs, nor the insertion of Polybia-MP1 into monolayers, and peptide-membrane affinity was higher for those with DP than with CHO. Zeta potentials (ζ) for DP-containing LUVs showed a complex behavior at increasing peptide concentration. The effect of the peptide on membrane elasticity, investigated by nanotube retraction experiments, showed that peptide addition softened all membrane compositions, but membranes with DP got stiffer at long times. Considering this, and the ζ results, we propose that peptides accumulate at the interface adopting different arrangements, leading to a non-monotonic behavior. Possible correlations with cell membranes were inquired testing the antimicrobial activity of Polybia-MP1 against hopanoid-lacking bacteria pre-incubated with DP or CHO. The fraction of surviving cells was lower in cultures incubated with DP compared to those incubated with CHO. We propose that the higher activity of Polybia-MP1 against some bacteria compared to mammalian cells is not only related to membrane electrostatics, but also the composition of neutral lipids, particularly the hopanoids, could be important.
publishDate 2021
dc.date.none.fl_str_mv 2021-01-01
2022-04-29T08:29:28Z
2022-04-29T08:29:28Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1016/j.bbadva.2021.100002
BBA Advances, v. 1.
2667-1603
http://hdl.handle.net/11449/228932
10.1016/j.bbadva.2021.100002
2-s2.0-85104980420
url http://dx.doi.org/10.1016/j.bbadva.2021.100002
http://hdl.handle.net/11449/228932
identifier_str_mv BBA Advances, v. 1.
2667-1603
10.1016/j.bbadva.2021.100002
2-s2.0-85104980420
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv BBA Advances
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
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