Disclosure of a promising lead to tackle complicated skin and skin structure infections: Antimicrobial and antibiofilm actions of peptide pp4-3.1
Autor(a) principal: | |
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Data de Publicação: | 2021 |
Outros Autores: | , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | https://hdl.handle.net/10216/155612 |
Resumo: | Efficient antibiotics are being exhausted, which compromises the treatment of infections, including complicated skin and skin structure infections (cSSTI) often associated with multidrug resistant (MDR) bacteria, methicillin-resistant S. aureus (MRSA) being the most prevalent. Antimi-crobial peptides (AMP) are being increasingly regarded as the new hope for the post-antibiotic era. Thus, future management of cSSTI may include use of peptides that, on the one hand, behave as AMP and, on the other, are able to promote fast and correct skin rebuilding. As such, we combined the well-known cosmeceutical pentapeptide-4 (PP4), devoid of antimicrobial action but possessing collagenesis-boosting properties, with the AMP 3.1, to afford the chimeric peptide PP4-3.1. We further produced its N-methyl imidazole derivative, MeIm-PP4-3.1. Both peptide-based constructs were evaluated in vitro against Gram-negative bacteria, Gram-positive bacteria, and Candida spp. fungi. Additionally, the antibiofilm activity, the toxicity to human keratinocytes, and the activity against S. aureus in simulated wound fluid (SWF) were assessed. The chimeric peptide PP4-3.1 stood out for its potent activity against Gram-positive and Gram-negative bacteria, including against MDR clinical isolates (0.8 = MIC = 5.7 µM), both in planktonic form and in biofilm matrix. The peptide was also active against three clinically relevant species of Candida fungi, with an overall performance superior to that of fluconazole. Altogether, data reveal that PP4-3.1 is as a promising lead for the future development of new topical treatments for severe skin infections. |
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Disclosure of a promising lead to tackle complicated skin and skin structure infections: Antimicrobial and antibiofilm actions of peptide pp4-3.1AntibacterialAntibiofilmAntifungalAntimicrobial peptidesCollagenMultidrug resis-tanceSkin infectionsWound healingEfficient antibiotics are being exhausted, which compromises the treatment of infections, including complicated skin and skin structure infections (cSSTI) often associated with multidrug resistant (MDR) bacteria, methicillin-resistant S. aureus (MRSA) being the most prevalent. Antimi-crobial peptides (AMP) are being increasingly regarded as the new hope for the post-antibiotic era. Thus, future management of cSSTI may include use of peptides that, on the one hand, behave as AMP and, on the other, are able to promote fast and correct skin rebuilding. As such, we combined the well-known cosmeceutical pentapeptide-4 (PP4), devoid of antimicrobial action but possessing collagenesis-boosting properties, with the AMP 3.1, to afford the chimeric peptide PP4-3.1. We further produced its N-methyl imidazole derivative, MeIm-PP4-3.1. Both peptide-based constructs were evaluated in vitro against Gram-negative bacteria, Gram-positive bacteria, and Candida spp. fungi. Additionally, the antibiofilm activity, the toxicity to human keratinocytes, and the activity against S. aureus in simulated wound fluid (SWF) were assessed. The chimeric peptide PP4-3.1 stood out for its potent activity against Gram-positive and Gram-negative bacteria, including against MDR clinical isolates (0.8 = MIC = 5.7 µM), both in planktonic form and in biofilm matrix. The peptide was also active against three clinically relevant species of Candida fungi, with an overall performance superior to that of fluconazole. Altogether, data reveal that PP4-3.1 is as a promising lead for the future development of new topical treatments for severe skin infections.MDPI20212021-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/10216/155612eng1999-492310.3390/pharmaceutics13111962Gomes, ABessa, LJFernandes, IFerraz, RMonteiro, CMartins, MCLMateus, NGameiro, PTeixeira, CGomes, Pinfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-09-27T09:04:11Zoai:repositorio-aberto.up.pt:10216/155612Portal AgregadorONGhttps://www.rcaap.pt/oai/openairemluisa.alvim@gmail.comopendoar:71602024-09-27T09:04:11Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Disclosure of a promising lead to tackle complicated skin and skin structure infections: Antimicrobial and antibiofilm actions of peptide pp4-3.1 |
title |
Disclosure of a promising lead to tackle complicated skin and skin structure infections: Antimicrobial and antibiofilm actions of peptide pp4-3.1 |
spellingShingle |
Disclosure of a promising lead to tackle complicated skin and skin structure infections: Antimicrobial and antibiofilm actions of peptide pp4-3.1 Gomes, A Antibacterial Antibiofilm Antifungal Antimicrobial peptides Collagen Multidrug resis-tance Skin infections Wound healing |
title_short |
Disclosure of a promising lead to tackle complicated skin and skin structure infections: Antimicrobial and antibiofilm actions of peptide pp4-3.1 |
title_full |
Disclosure of a promising lead to tackle complicated skin and skin structure infections: Antimicrobial and antibiofilm actions of peptide pp4-3.1 |
title_fullStr |
Disclosure of a promising lead to tackle complicated skin and skin structure infections: Antimicrobial and antibiofilm actions of peptide pp4-3.1 |
title_full_unstemmed |
Disclosure of a promising lead to tackle complicated skin and skin structure infections: Antimicrobial and antibiofilm actions of peptide pp4-3.1 |
title_sort |
Disclosure of a promising lead to tackle complicated skin and skin structure infections: Antimicrobial and antibiofilm actions of peptide pp4-3.1 |
author |
Gomes, A |
author_facet |
Gomes, A Bessa, LJ Fernandes, I Ferraz, R Monteiro, C Martins, MCL Mateus, N Gameiro, P Teixeira, C Gomes, P |
author_role |
author |
author2 |
Bessa, LJ Fernandes, I Ferraz, R Monteiro, C Martins, MCL Mateus, N Gameiro, P Teixeira, C Gomes, P |
author2_role |
author author author author author author author author author |
dc.contributor.author.fl_str_mv |
Gomes, A Bessa, LJ Fernandes, I Ferraz, R Monteiro, C Martins, MCL Mateus, N Gameiro, P Teixeira, C Gomes, P |
dc.subject.por.fl_str_mv |
Antibacterial Antibiofilm Antifungal Antimicrobial peptides Collagen Multidrug resis-tance Skin infections Wound healing |
topic |
Antibacterial Antibiofilm Antifungal Antimicrobial peptides Collagen Multidrug resis-tance Skin infections Wound healing |
description |
Efficient antibiotics are being exhausted, which compromises the treatment of infections, including complicated skin and skin structure infections (cSSTI) often associated with multidrug resistant (MDR) bacteria, methicillin-resistant S. aureus (MRSA) being the most prevalent. Antimi-crobial peptides (AMP) are being increasingly regarded as the new hope for the post-antibiotic era. Thus, future management of cSSTI may include use of peptides that, on the one hand, behave as AMP and, on the other, are able to promote fast and correct skin rebuilding. As such, we combined the well-known cosmeceutical pentapeptide-4 (PP4), devoid of antimicrobial action but possessing collagenesis-boosting properties, with the AMP 3.1, to afford the chimeric peptide PP4-3.1. We further produced its N-methyl imidazole derivative, MeIm-PP4-3.1. Both peptide-based constructs were evaluated in vitro against Gram-negative bacteria, Gram-positive bacteria, and Candida spp. fungi. Additionally, the antibiofilm activity, the toxicity to human keratinocytes, and the activity against S. aureus in simulated wound fluid (SWF) were assessed. The chimeric peptide PP4-3.1 stood out for its potent activity against Gram-positive and Gram-negative bacteria, including against MDR clinical isolates (0.8 = MIC = 5.7 µM), both in planktonic form and in biofilm matrix. The peptide was also active against three clinically relevant species of Candida fungi, with an overall performance superior to that of fluconazole. Altogether, data reveal that PP4-3.1 is as a promising lead for the future development of new topical treatments for severe skin infections. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021 2021-01-01T00:00:00Z |
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 |
https://hdl.handle.net/10216/155612 |
url |
https://hdl.handle.net/10216/155612 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
1999-4923 10.3390/pharmaceutics13111962 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
MDPI |
publisher.none.fl_str_mv |
MDPI |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
repository.mail.fl_str_mv |
mluisa.alvim@gmail.com |
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1817548141786824704 |