دورية أكاديمية
أعرض في EDS

Antimicrobial Spectrum of Activity and Mechanism of Action of Linear Alpha-Helical Peptides Inspired by Shrimp Anti-Lipopolysaccharide Factors.

التفاصيل البيبلوغرافية
العنوان: Antimicrobial Spectrum of Activity and Mechanism of Action of Linear Alpha-Helical Peptides Inspired by Shrimp Anti-Lipopolysaccharide Factors.
المؤلفون: Matos GM; Laboratory of Immunology Applied to Aquaculture, Department of Cell Biology, Embryology and Genetics, Federal University of Santa Catarina, Florianópolis 88040-900, Brazil., Garcia-Teodoro B; Laboratory of Immunology Applied to Aquaculture, Department of Cell Biology, Embryology and Genetics, Federal University of Santa Catarina, Florianópolis 88040-900, Brazil., Martins CP; Laboratory of Immunology Applied to Aquaculture, Department of Cell Biology, Embryology and Genetics, Federal University of Santa Catarina, Florianópolis 88040-900, Brazil., Schmitt P; Laboratorio de Genética e Inmunología Molecular, Instituto de Biología, Facultad de Ciencias, Pontificia Universidad Católica de Valparaíso, Valparaíso 2373223, Chile., Guzmán F; Núcleo Biotecnología Curauma, Pontificia Universidad Católica de Valparaíso, Valparaíso 2373223, Chile., de Freitas ACO; Laboratory of Protozoology, Department of Microbiology, Parasitology and Immunology, Federal University of Santa Catarina, Florianópolis 88040-900, Brazil., Stoco PH; Laboratory of Protozoology, Department of Microbiology, Parasitology and Immunology, Federal University of Santa Catarina, Florianópolis 88040-900, Brazil., Ferreira FA; Laboratory of Molecular Genetics of Bacteria, Department of Microbiology, Parasitology and Immunology, Federal University of Santa Catarina, Florianópolis 88040-900, Brazil., Stadnik MJ; Laboratory of Plant Pathology, Department of Plant Sciences, Federal University of Santa Catarina, Florianópolis 88034-001, Brazil., Robl D; Laboratory of Microorganisms and Biotechnological Processes, Department of Microbiology, Parasitology and Immunology, Federal University of Santa Catarina, Florianópolis 88040-900, Brazil., Perazzolo LM; Laboratory of Immunology Applied to Aquaculture, Department of Cell Biology, Embryology and Genetics, Federal University of Santa Catarina, Florianópolis 88040-900, Brazil., Rosa RD; Laboratory of Immunology Applied to Aquaculture, Department of Cell Biology, Embryology and Genetics, Federal University of Santa Catarina, Florianópolis 88040-900, Brazil.
المصدر: Biomolecules [Biomolecules] 2023 Jan 11; Vol. 13 (1). Date of Electronic Publication: 2023 Jan 11.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: MDPI Country of Publication: Switzerland NLM ID: 101596414 Publication Model: Electronic Cited Medium: Internet ISSN: 2218-273X (Electronic) Linking ISSN: 2218273X NLM ISO Abbreviation: Biomolecules Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Basel, Switzerland : MDPI, 2011-
مواضيع طبية MeSH: Anti-Bacterial Agents*/pharmacology , Anti-Infective Agents*/chemistry, Humans ; Protein Conformation, alpha-Helical ; Lipopolysaccharides/pharmacology ; Gram-Negative Bacteria ; Gram-Positive Bacteria ; Antimicrobial Cationic Peptides/pharmacology ; Antimicrobial Cationic Peptides/chemistry ; Microbial Sensitivity Tests
مستخلص: Shrimp antilipopolysaccharide factors (ALFs) form a multifunctional and diverse family of antimicrobial host defense peptides (AMPs) composed of seven members (groups A to G), which differ in terms of their primary structure and biochemical properties. They are amphipathic peptides with two conserved cysteine residues stabilizing a central β-hairpin that is understood to be the core region for their biological activities. In this study, we synthetized three linear (cysteine-free) peptides based on the amino acid sequence of the central β-hairpin of the newly identified shrimp ( Litopenaeus vannamei ) ALFs from groups E to G. Unlike whole mature ALFs, the ALF-derived peptides exhibited an α-helix secondary structure. In vitro assays revealed that the synthetic peptides display a broad spectrum of activity against both Gram-positive and Gram-negative bacteria and fungi but not against the protozoan parasites Trypanosoma cruzi and Leishmania ( L .) infantum . Remarkably, they displayed synergistic effects and showed the ability to permeabilize bacterial membranes, a mechanism of action of classical AMPs. Having shown low cytotoxicity to THP-1 human cells and being active against clinical multiresistant bacterial isolates, these nature-inspired peptides represent an interesting class of bioactive molecules with biotechnological potential for the development of novel therapeutics in medical sciences.
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معلومات مُعتمدة: 406530/2016-5, 304352/2019-5 and 312047/2021-5 National Council for Scientific and Technological Development; 1974/2014 Coordenação de Aperfeicoamento de Pessoal de Nível Superior; 1200129 FONDECYT
فهرسة مساهمة: Keywords: antibacterial; antifungal; antimicrobial peptide (AMP); antiparasitic activity; crustacean; cytotoxicity; host defense peptide (HDP); membrane-disrupting; methicillin-resistant Staphylococcus aureus (MRSA); synergy
المشرفين على المادة: 0 (Anti-Bacterial Agents)
0 (Lipopolysaccharides)
0 (Anti-Infective Agents)
0 (Antimicrobial Cationic Peptides)
تواريخ الأحداث: Date Created: 20230121 Date Completed: 20230124 Latest Revision: 20230213
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC9856130
DOI: 10.3390/biom13010150
PMID: 36671535
قاعدة البيانات: MEDLINE
الوصف
تدمد:2218-273X
DOI:10.3390/biom13010150