The antimicrobial peptide Polybia-MP1 differentiates membranes with the hopanoid, diplopterol from those with cholesterol
Autor(a) principal: | |
---|---|
Data de Publicação: | 2021 |
Outros Autores: | , , |
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. |
id |
UNSP_49f482e1c1e9f2a0545a15966b009873 |
---|---|
oai_identifier_str |
oai:repositorio.unesp.br:11449/228932 |
network_acronym_str |
UNSP |
network_name_str |
Repositório Institucional da UNESP |
repository_id_str |
2946 |
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) |
repository.mail.fl_str_mv |
|
_version_ |
1808129579208933376 |