Understanding the mechanism of action of peptide (p-BthTX-I)2 derived from C-terminal region of phospholipase A2 (PLA2)-like bothropstoxin-I on Gram-positive and Gram-negative bacteria

Detalhes bibliográficos
Autor(a) principal: Santos-Filho, Norival Alves [UNESP]
Data de Publicação: 2021
Outros Autores: de Freitas, Laura Marise [UNESP], Santos, Claudia Tavares dos [UNESP], Piccoli, Julia Pinto [UNESP], Fontana, Carla Raquel [UNESP], Fusco-Almeida, Ana Marisa [UNESP], Cilli, Eduardo Maffud [UNESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1016/j.toxicon.2021.03.015
http://hdl.handle.net/11449/207575
Resumo: Based on the antimicrobial activity of bothropstoxin-I (BthTX-I) and on the premise that a C-terminal peptide of Lys49 myotoxin can reproduce the antimicrobial activity of the parent protein, we aimed to study the mechanism of action of a peptide derived from the C-terminal region of the myotoxin BthTX-I [(p-BthTX-I)2, sequence: KKYRYHLKPFCKK, disulfide-linked dimer] against Gram-positive and Gram-negative bacteria. Fluorescence quenching technique showed that the carboxyfluorescein labeled-peptide [CF-(p-BthTX-I)2] when incubated with E. coli displayed a superior penetration activity than when incubated with S. aureus. Cell death induced by the peptide (p-BthTX-I)2 showed a loss of membrane integrity in E. coli and S. aureus; however, the mechanisms of cell death were different, characterized by the presence of necrosis-like and apoptosis-like deaths, respectively. Scanning electron microscopy studies in E. coli and S. aureus showed morphological changes in the cells, with superficial deformities, appearance of wrinkles and bubbles, and formation of vesicles. Our results demonstrate that the mechanism of action of the peptide (p-BthTX-I)2 is different in Gram-negative (E. coli) and Gram-positive (S. aureus) bacteria. Knowledge of the mechanism of action of these peptides is important, since they are promising prototypes for new antimicrobial drugs.
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spelling Understanding the mechanism of action of peptide (p-BthTX-I)2 derived from C-terminal region of phospholipase A2 (PLA2)-like bothropstoxin-I on Gram-positive and Gram-negative bacteriaAntimicrobial peptidesBthTX-ICarboxyfluorescein labeled-peptideFlow cytometryPhospholypase A2Scanning electron microscopyBased on the antimicrobial activity of bothropstoxin-I (BthTX-I) and on the premise that a C-terminal peptide of Lys49 myotoxin can reproduce the antimicrobial activity of the parent protein, we aimed to study the mechanism of action of a peptide derived from the C-terminal region of the myotoxin BthTX-I [(p-BthTX-I)2, sequence: KKYRYHLKPFCKK, disulfide-linked dimer] against Gram-positive and Gram-negative bacteria. Fluorescence quenching technique showed that the carboxyfluorescein labeled-peptide [CF-(p-BthTX-I)2] when incubated with E. coli displayed a superior penetration activity than when incubated with S. aureus. Cell death induced by the peptide (p-BthTX-I)2 showed a loss of membrane integrity in E. coli and S. aureus; however, the mechanisms of cell death were different, characterized by the presence of necrosis-like and apoptosis-like deaths, respectively. Scanning electron microscopy studies in E. coli and S. aureus showed morphological changes in the cells, with superficial deformities, appearance of wrinkles and bubbles, and formation of vesicles. Our results demonstrate that the mechanism of action of the peptide (p-BthTX-I)2 is different in Gram-negative (E. coli) and Gram-positive (S. aureus) bacteria. Knowledge of the mechanism of action of these peptides is important, since they are promising prototypes for new antimicrobial drugs.Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Instituto de Química Universidade Estadual Paulista (UNESP)Campus Experimental de Registro Universidade Estadual Paulista (UNESP)Faculdade de Ciências Farmacêuticas Universidade Estadual Paulista (UNESP)Instituto de Química Depto de Bioquímica Universidade de São Paulo (USP), São PauloInstituto de Química Universidade Estadual Paulista (UNESP)Campus Experimental de Registro Universidade Estadual Paulista (UNESP)Faculdade de Ciências Farmacêuticas Universidade Estadual Paulista (UNESP)FAPESP: #2013/07600-3FAPESP: #2014/05538-1FAPESP: #2014/24581-5Universidade Estadual Paulista (Unesp)Universidade de São Paulo (USP)Santos-Filho, Norival Alves [UNESP]de Freitas, Laura Marise [UNESP]Santos, Claudia Tavares dos [UNESP]Piccoli, Julia Pinto [UNESP]Fontana, Carla Raquel [UNESP]Fusco-Almeida, Ana Marisa [UNESP]Cilli, Eduardo Maffud [UNESP]2021-06-25T10:57:28Z2021-06-25T10:57:28Z2021-06-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article44-55http://dx.doi.org/10.1016/j.toxicon.2021.03.015Toxicon, v. 196, p. 44-55.1879-31500041-0101http://hdl.handle.net/11449/20757510.1016/j.toxicon.2021.03.0152-s2.0-85103789344Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengToxiconinfo:eu-repo/semantics/openAccess2024-05-03T13:20:09Zoai:repositorio.unesp.br:11449/207575Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T18:54:51.273516Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Understanding the mechanism of action of peptide (p-BthTX-I)2 derived from C-terminal region of phospholipase A2 (PLA2)-like bothropstoxin-I on Gram-positive and Gram-negative bacteria
title Understanding the mechanism of action of peptide (p-BthTX-I)2 derived from C-terminal region of phospholipase A2 (PLA2)-like bothropstoxin-I on Gram-positive and Gram-negative bacteria
spellingShingle Understanding the mechanism of action of peptide (p-BthTX-I)2 derived from C-terminal region of phospholipase A2 (PLA2)-like bothropstoxin-I on Gram-positive and Gram-negative bacteria
Santos-Filho, Norival Alves [UNESP]
Antimicrobial peptides
BthTX-I
Carboxyfluorescein labeled-peptide
Flow cytometry
Phospholypase A2
Scanning electron microscopy
title_short Understanding the mechanism of action of peptide (p-BthTX-I)2 derived from C-terminal region of phospholipase A2 (PLA2)-like bothropstoxin-I on Gram-positive and Gram-negative bacteria
title_full Understanding the mechanism of action of peptide (p-BthTX-I)2 derived from C-terminal region of phospholipase A2 (PLA2)-like bothropstoxin-I on Gram-positive and Gram-negative bacteria
title_fullStr Understanding the mechanism of action of peptide (p-BthTX-I)2 derived from C-terminal region of phospholipase A2 (PLA2)-like bothropstoxin-I on Gram-positive and Gram-negative bacteria
title_full_unstemmed Understanding the mechanism of action of peptide (p-BthTX-I)2 derived from C-terminal region of phospholipase A2 (PLA2)-like bothropstoxin-I on Gram-positive and Gram-negative bacteria
title_sort Understanding the mechanism of action of peptide (p-BthTX-I)2 derived from C-terminal region of phospholipase A2 (PLA2)-like bothropstoxin-I on Gram-positive and Gram-negative bacteria
author Santos-Filho, Norival Alves [UNESP]
author_facet Santos-Filho, Norival Alves [UNESP]
de Freitas, Laura Marise [UNESP]
Santos, Claudia Tavares dos [UNESP]
Piccoli, Julia Pinto [UNESP]
Fontana, Carla Raquel [UNESP]
Fusco-Almeida, Ana Marisa [UNESP]
Cilli, Eduardo Maffud [UNESP]
author_role author
author2 de Freitas, Laura Marise [UNESP]
Santos, Claudia Tavares dos [UNESP]
Piccoli, Julia Pinto [UNESP]
Fontana, Carla Raquel [UNESP]
Fusco-Almeida, Ana Marisa [UNESP]
Cilli, Eduardo Maffud [UNESP]
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (Unesp)
Universidade de São Paulo (USP)
dc.contributor.author.fl_str_mv Santos-Filho, Norival Alves [UNESP]
de Freitas, Laura Marise [UNESP]
Santos, Claudia Tavares dos [UNESP]
Piccoli, Julia Pinto [UNESP]
Fontana, Carla Raquel [UNESP]
Fusco-Almeida, Ana Marisa [UNESP]
Cilli, Eduardo Maffud [UNESP]
dc.subject.por.fl_str_mv Antimicrobial peptides
BthTX-I
Carboxyfluorescein labeled-peptide
Flow cytometry
Phospholypase A2
Scanning electron microscopy
topic Antimicrobial peptides
BthTX-I
Carboxyfluorescein labeled-peptide
Flow cytometry
Phospholypase A2
Scanning electron microscopy
description Based on the antimicrobial activity of bothropstoxin-I (BthTX-I) and on the premise that a C-terminal peptide of Lys49 myotoxin can reproduce the antimicrobial activity of the parent protein, we aimed to study the mechanism of action of a peptide derived from the C-terminal region of the myotoxin BthTX-I [(p-BthTX-I)2, sequence: KKYRYHLKPFCKK, disulfide-linked dimer] against Gram-positive and Gram-negative bacteria. Fluorescence quenching technique showed that the carboxyfluorescein labeled-peptide [CF-(p-BthTX-I)2] when incubated with E. coli displayed a superior penetration activity than when incubated with S. aureus. Cell death induced by the peptide (p-BthTX-I)2 showed a loss of membrane integrity in E. coli and S. aureus; however, the mechanisms of cell death were different, characterized by the presence of necrosis-like and apoptosis-like deaths, respectively. Scanning electron microscopy studies in E. coli and S. aureus showed morphological changes in the cells, with superficial deformities, appearance of wrinkles and bubbles, and formation of vesicles. Our results demonstrate that the mechanism of action of the peptide (p-BthTX-I)2 is different in Gram-negative (E. coli) and Gram-positive (S. aureus) bacteria. Knowledge of the mechanism of action of these peptides is important, since they are promising prototypes for new antimicrobial drugs.
publishDate 2021
dc.date.none.fl_str_mv 2021-06-25T10:57:28Z
2021-06-25T10:57:28Z
2021-06-01
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/10.1016/j.toxicon.2021.03.015
Toxicon, v. 196, p. 44-55.
1879-3150
0041-0101
http://hdl.handle.net/11449/207575
10.1016/j.toxicon.2021.03.015
2-s2.0-85103789344
url http://dx.doi.org/10.1016/j.toxicon.2021.03.015
http://hdl.handle.net/11449/207575
identifier_str_mv Toxicon, v. 196, p. 44-55.
1879-3150
0041-0101
10.1016/j.toxicon.2021.03.015
2-s2.0-85103789344
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Toxicon
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 44-55
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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