Disclosure of a promising lead to tackle complicated skin and skin structure infections: Antimicrobial and antibiofilm actions of peptide pp4-3.1

Detalhes bibliográficos
Autor(a) principal: Gomes, A
Data de Publicação: 2021
Outros Autores: Bessa, LJ, Fernandes, I, Ferraz, R, Monteiro, C, Martins, MCL, Mateus, N, Gameiro, P, Teixeira, C, Gomes, P
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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spelling 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:RCAAP2023-12-16T06:03:23Zoai:repositorio-aberto.up.pt:10216/155612Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T00:54:33.649630Repositório 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
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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
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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
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instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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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
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