دورية أكاديمية
Anti-Staphy Peptides Rationally Designed from Cry10Aa Bacterial Protein.
العنوان: | Anti-Staphy Peptides Rationally Designed from Cry10Aa Bacterial Protein. |
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المؤلفون: | Rios TB; S-Inova Biotech, Programa de Pós-Graduação em Biotecnologia Universidade Católica Dom Bosco, Av. Tamandaré, 6000-Jardim Seminario, Campo Grande, MS 79117-900, Brazil.; Centro de Análises Proteômicas e Bioquímicas, Programa de Pós-Graduação em Ciências Genômicas e Biotecnologia Universidade Católica de Brasília, St. de Grandes Áreas Norte 916-Asa Norte, Brasília, DF 70790-160, Brazil., Maximiano MR; S-Inova Biotech, Programa de Pós-Graduação em Biotecnologia Universidade Católica Dom Bosco, Av. Tamandaré, 6000-Jardim Seminario, Campo Grande, MS 79117-900, Brazil.; Centro de Análises Proteômicas e Bioquímicas, Programa de Pós-Graduação em Ciências Genômicas e Biotecnologia Universidade Católica de Brasília, St. de Grandes Áreas Norte 916-Asa Norte, Brasília, DF 70790-160, Brazil., Fernandes FC; Centro de Análises Proteômicas e Bioquímicas, Programa de Pós-Graduação em Ciências Genômicas e Biotecnologia Universidade Católica de Brasília, St. de Grandes Áreas Norte 916-Asa Norte, Brasília, DF 70790-160, Brazil., Amorim GC; Centro de Análises Proteômicas e Bioquímicas, Programa de Pós-Graduação em Ciências Genômicas e Biotecnologia Universidade Católica de Brasília, St. de Grandes Áreas Norte 916-Asa Norte, Brasília, DF 70790-160, Brazil.; Embrapa Recursos Genéticos e Biotecnologia, Parque Estação Biológica, PqEB, Av. W5 Norte-Asa Norte, Brasília, DF 70770-917, Brazil., Porto WF; Porto Reports, Brasília, DF 70770-917, Brazil., Buccini DF; S-Inova Biotech, Programa de Pós-Graduação em Biotecnologia Universidade Católica Dom Bosco, Av. Tamandaré, 6000-Jardim Seminario, Campo Grande, MS 79117-900, Brazil., Nieto Marín V; S-Inova Biotech, Programa de Pós-Graduação em Biotecnologia Universidade Católica Dom Bosco, Av. Tamandaré, 6000-Jardim Seminario, Campo Grande, MS 79117-900, Brazil., Feitosa GC; Centro de Análises Proteômicas e Bioquímicas, Programa de Pós-Graduação em Ciências Genômicas e Biotecnologia Universidade Católica de Brasília, St. de Grandes Áreas Norte 916-Asa Norte, Brasília, DF 70790-160, Brazil.; Pós-Graduação em Patologia Molecular, Universidade de Brasília, Campus Darcy Ribeiro, Brasília, DF 70910-900, Brazil., Freitas CDP; Laboratório de RMN, Instituto de Química, Universidade Federal de Goiás, Goiânia, GO 74690-900, Brazil., Barra JB; Laboratório de RMN, Instituto de Química, Universidade Federal de Goiás, Goiânia, GO 74690-900, Brazil., Alonso A; Instituto de Física, Universidade Federal de Goiás, Goiânia, GO 74690-900, Brazil., Grossi de Sá MF; Centro de Análises Proteômicas e Bioquímicas, Programa de Pós-Graduação em Ciências Genômicas e Biotecnologia Universidade Católica de Brasília, St. de Grandes Áreas Norte 916-Asa Norte, Brasília, DF 70790-160, Brazil.; Embrapa Recursos Genéticos e Biotecnologia, Parque Estação Biológica, PqEB, Av. W5 Norte-Asa Norte, Brasília, DF 70770-917, Brazil., Lião LM; Laboratório de RMN, Instituto de Química, Universidade Federal de Goiás, Goiânia, GO 74690-900, Brazil., Franco OL; S-Inova Biotech, Programa de Pós-Graduação em Biotecnologia Universidade Católica Dom Bosco, Av. Tamandaré, 6000-Jardim Seminario, Campo Grande, MS 79117-900, Brazil.; Centro de Análises Proteômicas e Bioquímicas, Programa de Pós-Graduação em Ciências Genômicas e Biotecnologia Universidade Católica de Brasília, St. de Grandes Áreas Norte 916-Asa Norte, Brasília, DF 70790-160, Brazil. |
المصدر: | ACS omega [ACS Omega] 2024 Jun 19; Vol. 9 (27), pp. 29159-29174. Date of Electronic Publication: 2024 Jun 19 (Print Publication: 2024). |
نوع المنشور: | Journal Article |
اللغة: | English |
بيانات الدورية: | Publisher: American Chemical Society Country of Publication: United States NLM ID: 101691658 Publication Model: eCollection Cited Medium: Internet ISSN: 2470-1343 (Electronic) Linking ISSN: 24701343 NLM ISO Abbreviation: ACS Omega Subsets: PubMed not MEDLINE |
أسماء مطبوعة: | Original Publication: Washington, D.C. : American Chemical Society, [2016]- |
مستخلص: | Bacterial infections pose a significant threat to human health, constituting a major challenge for healthcare systems. Antibiotic resistance is particularly concerning in the context of treating staphylococcal infections. In addressing this challenge, antimicrobial peptides (AMPs), characterized by their hydrophobic and cationic properties, unique mechanism of action, and remarkable bactericidal and immunomodulatory capabilities, emerge as promising alternatives to conventional antibiotics for tackling bacterial multidrug resistance. This study focuses on the Cry10Aa protein as a template for generating AMPs due to its membrane-penetrating ability. Leveraging the Joker algorithm, six peptide variants were derived from α-helix 3 of Cry10Aa, known for its interaction with lipid bilayers. In vitro, antimicrobial assays determined the minimum inhibitory concentration (MIC) and minimum bactericidal concentration (MBC) required for inhibiting the growth of Staphylococcus aureus , Escherichia coli , Acinetobacter baummanii , Enterobacter cloacae , Enterococcus facallis , Klebsiella pneumonia , and Pseudomonas aeruginosa . Time-kill kinetics were performed using the parental peptide AMPCry10Aa, as well as AMPCry10Aa_1 and AMPCry10Aa_5, against E. coli ATCC, S. aureus 111 and S. aureus ATCC strains showing that AMPCry10Aa_1 and AMPCry10Aa_5 peptides can completely reduce the initial bacterial load with less than 2 h of incubation. AMPCry10Aa_1 and AMPCry 10Aa_5 present stability in human serum and activity maintenance up to 37 °C. Cytotoxicity assays, conducted using the MTT method, revealed that all of the tested peptides exhibited cell viability >50% (IC50). The study also encompassed evaluations of the structure and physical-chemical properties. The three-dimensional structures of AMPCry10Aa and AMPCry10Aa_5 were determined through nuclear magnetic resonance (NMR) spectroscopy, indicating the adoption of α-helical segments. Electron paramagnetic resonance (EPR) spectroscopy elucidated the mechanism of action, demonstrating that AMPCry10Aa_5 enters the outer membranes of E. coli and S. aureus , causing substantial increases in lipid fluidity, while AMPCry10Aa slightly increases lipid fluidity in E. coli . In conclusion, the results obtained underscore the potential of Cry10Aa as a source for developing antimicrobial peptides as alternatives to conventional antibiotics, offering a promising avenue in the battle against antibiotic resistance. Competing Interests: The authors declare no competing financial interest. (© 2024 The Authors. Published by American Chemical Society.) |
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تواريخ الأحداث: | Date Created: 20240715 Latest Revision: 20240716 |
رمز التحديث: | 20240716 |
مُعرف محوري في PubMed: | PMC11238290 |
DOI: | 10.1021/acsomega.3c07455 |
PMID: | 39005792 |
قاعدة البيانات: | MEDLINE |
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