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
Autor(a) principal: | |
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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.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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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 |
|
_version_ |
1808128998667976704 |