The effect of acidic pH on the adsorption and lytic activity of the peptides Polybia-MP1 and its histidine-containing analog in anionic lipid membrane: a biophysical study by molecular dynamics and spectroscopy

Detalhes bibliográficos
Autor(a) principal: Martins, Ingrid Bernardes Santana [UNESP]
Data de Publicação: 2021
Outros Autores: Viegas, Taisa Giordano [UNESP], dos Santos Alvares, Dayane [UNESP], de Souza, Bibiana Monson [UNESP], Palma, Mário Sérgio [UNESP], Ruggiero Neto, João [UNESP], de Araujo, Alexandre Suman [UNESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1007/s00726-021-02982-0
http://hdl.handle.net/11449/207666
Resumo: Antimicrobial peptides (AMPs) are part of the innate immune system of many species. AMPs are short sequences rich in charged and non-polar residues. They act on the lipid phase of the plasma membrane without requiring membrane receptors. Polybia-MP1 (MP1), extracted from a native wasp, is a broad-spectrum bactericide, an inhibitor of cancer cell proliferation being non-hemolytic and non-cytotoxic. MP1 mechanism of action and its adsorption mode is not yet completely known. Its adsorption to lipid bilayer and lytic activity is most likely dependent on the ionization state of its two acidic and three basic residues and consequently on the bulk pH. Here we investigated the effect of bulk acidic (pH 5.5) and neutral pH (7.4) solution on the adsorption, insertion, and lytic activity of MP1 and its analog H-MP1 to anionic (7POPC:3POPG) model membrane. H-MP1 is a synthetic analog of MP1 with lysines replaced by histidines. Bulk pH changes could modulate this peptide efficiency. The combination of different experimental techniques and molecular dynamics (MD) simulations showed that the adsorption, insertion, and lytic activity of H-MP1 are highly sensitive to bulk pH in opposition to MP1. The atomistic details, provided by MD simulations, showed peptides contact their N-termini to the bilayer before the insertion and then lay parallel to the bilayer. Their hydrophobic faces inserted into the acyl chain phase disturb the lipid-packing.
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spelling The effect of acidic pH on the adsorption and lytic activity of the peptides Polybia-MP1 and its histidine-containing analog in anionic lipid membrane: a biophysical study by molecular dynamics and spectroscopyAntimicrobial peptidesConformational analysisLytic activityMolecular dynamics simulationpH sensitive peptideAntimicrobial peptides (AMPs) are part of the innate immune system of many species. AMPs are short sequences rich in charged and non-polar residues. They act on the lipid phase of the plasma membrane without requiring membrane receptors. Polybia-MP1 (MP1), extracted from a native wasp, is a broad-spectrum bactericide, an inhibitor of cancer cell proliferation being non-hemolytic and non-cytotoxic. MP1 mechanism of action and its adsorption mode is not yet completely known. Its adsorption to lipid bilayer and lytic activity is most likely dependent on the ionization state of its two acidic and three basic residues and consequently on the bulk pH. Here we investigated the effect of bulk acidic (pH 5.5) and neutral pH (7.4) solution on the adsorption, insertion, and lytic activity of MP1 and its analog H-MP1 to anionic (7POPC:3POPG) model membrane. H-MP1 is a synthetic analog of MP1 with lysines replaced by histidines. Bulk pH changes could modulate this peptide efficiency. The combination of different experimental techniques and molecular dynamics (MD) simulations showed that the adsorption, insertion, and lytic activity of H-MP1 are highly sensitive to bulk pH in opposition to MP1. The atomistic details, provided by MD simulations, showed peptides contact their N-termini to the bilayer before the insertion and then lay parallel to the bilayer. Their hydrophobic faces inserted into the acyl chain phase disturb the lipid-packing.Department of Physics IBILCE UNESP-São Paulo State University, Cristóvão Colombo, 2265-Jardim NazarethDepartment of Basic and Applied Biology Institute of Biosciences UNESP-São Paulo State UniversityDepartment of Physics IBILCE UNESP-São Paulo State University, Cristóvão Colombo, 2265-Jardim NazarethDepartment of Basic and Applied Biology Institute of Biosciences UNESP-São Paulo State UniversityUniversidade Estadual Paulista (Unesp)Martins, Ingrid Bernardes Santana [UNESP]Viegas, Taisa Giordano [UNESP]dos Santos Alvares, Dayane [UNESP]de Souza, Bibiana Monson [UNESP]Palma, Mário Sérgio [UNESP]Ruggiero Neto, João [UNESP]de Araujo, Alexandre Suman [UNESP]2021-06-25T10:59:01Z2021-06-25T10:59:01Z2021-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1007/s00726-021-02982-0Amino Acids.1438-21990939-4451http://hdl.handle.net/11449/20766610.1007/s00726-021-02982-02-s2.0-85104994944Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengAmino Acidsinfo:eu-repo/semantics/openAccess2021-10-23T17:45:55Zoai:repositorio.unesp.br:11449/207666Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T19:35:39.217070Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv The effect of acidic pH on the adsorption and lytic activity of the peptides Polybia-MP1 and its histidine-containing analog in anionic lipid membrane: a biophysical study by molecular dynamics and spectroscopy
title The effect of acidic pH on the adsorption and lytic activity of the peptides Polybia-MP1 and its histidine-containing analog in anionic lipid membrane: a biophysical study by molecular dynamics and spectroscopy
spellingShingle The effect of acidic pH on the adsorption and lytic activity of the peptides Polybia-MP1 and its histidine-containing analog in anionic lipid membrane: a biophysical study by molecular dynamics and spectroscopy
Martins, Ingrid Bernardes Santana [UNESP]
Antimicrobial peptides
Conformational analysis
Lytic activity
Molecular dynamics simulation
pH sensitive peptide
title_short The effect of acidic pH on the adsorption and lytic activity of the peptides Polybia-MP1 and its histidine-containing analog in anionic lipid membrane: a biophysical study by molecular dynamics and spectroscopy
title_full The effect of acidic pH on the adsorption and lytic activity of the peptides Polybia-MP1 and its histidine-containing analog in anionic lipid membrane: a biophysical study by molecular dynamics and spectroscopy
title_fullStr The effect of acidic pH on the adsorption and lytic activity of the peptides Polybia-MP1 and its histidine-containing analog in anionic lipid membrane: a biophysical study by molecular dynamics and spectroscopy
title_full_unstemmed The effect of acidic pH on the adsorption and lytic activity of the peptides Polybia-MP1 and its histidine-containing analog in anionic lipid membrane: a biophysical study by molecular dynamics and spectroscopy
title_sort The effect of acidic pH on the adsorption and lytic activity of the peptides Polybia-MP1 and its histidine-containing analog in anionic lipid membrane: a biophysical study by molecular dynamics and spectroscopy
author Martins, Ingrid Bernardes Santana [UNESP]
author_facet Martins, Ingrid Bernardes Santana [UNESP]
Viegas, Taisa Giordano [UNESP]
dos Santos Alvares, Dayane [UNESP]
de Souza, Bibiana Monson [UNESP]
Palma, Mário Sérgio [UNESP]
Ruggiero Neto, João [UNESP]
de Araujo, Alexandre Suman [UNESP]
author_role author
author2 Viegas, Taisa Giordano [UNESP]
dos Santos Alvares, Dayane [UNESP]
de Souza, Bibiana Monson [UNESP]
Palma, Mário Sérgio [UNESP]
Ruggiero Neto, João [UNESP]
de Araujo, Alexandre Suman [UNESP]
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (Unesp)
dc.contributor.author.fl_str_mv Martins, Ingrid Bernardes Santana [UNESP]
Viegas, Taisa Giordano [UNESP]
dos Santos Alvares, Dayane [UNESP]
de Souza, Bibiana Monson [UNESP]
Palma, Mário Sérgio [UNESP]
Ruggiero Neto, João [UNESP]
de Araujo, Alexandre Suman [UNESP]
dc.subject.por.fl_str_mv Antimicrobial peptides
Conformational analysis
Lytic activity
Molecular dynamics simulation
pH sensitive peptide
topic Antimicrobial peptides
Conformational analysis
Lytic activity
Molecular dynamics simulation
pH sensitive peptide
description Antimicrobial peptides (AMPs) are part of the innate immune system of many species. AMPs are short sequences rich in charged and non-polar residues. They act on the lipid phase of the plasma membrane without requiring membrane receptors. Polybia-MP1 (MP1), extracted from a native wasp, is a broad-spectrum bactericide, an inhibitor of cancer cell proliferation being non-hemolytic and non-cytotoxic. MP1 mechanism of action and its adsorption mode is not yet completely known. Its adsorption to lipid bilayer and lytic activity is most likely dependent on the ionization state of its two acidic and three basic residues and consequently on the bulk pH. Here we investigated the effect of bulk acidic (pH 5.5) and neutral pH (7.4) solution on the adsorption, insertion, and lytic activity of MP1 and its analog H-MP1 to anionic (7POPC:3POPG) model membrane. H-MP1 is a synthetic analog of MP1 with lysines replaced by histidines. Bulk pH changes could modulate this peptide efficiency. The combination of different experimental techniques and molecular dynamics (MD) simulations showed that the adsorption, insertion, and lytic activity of H-MP1 are highly sensitive to bulk pH in opposition to MP1. The atomistic details, provided by MD simulations, showed peptides contact their N-termini to the bilayer before the insertion and then lay parallel to the bilayer. Their hydrophobic faces inserted into the acyl chain phase disturb the lipid-packing.
publishDate 2021
dc.date.none.fl_str_mv 2021-06-25T10:59:01Z
2021-06-25T10:59:01Z
2021-01-01
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/10.1007/s00726-021-02982-0
Amino Acids.
1438-2199
0939-4451
http://hdl.handle.net/11449/207666
10.1007/s00726-021-02982-0
2-s2.0-85104994944
url http://dx.doi.org/10.1007/s00726-021-02982-0
http://hdl.handle.net/11449/207666
identifier_str_mv Amino Acids.
1438-2199
0939-4451
10.1007/s00726-021-02982-0
2-s2.0-85104994944
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Amino Acids
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
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