Bioactivity and the First Transmission Electron Microscopy Immunogold Studies of Short De Novo -Designed Antimicrobial Peptides
| Autor: | Marisa Ann Azad, Cynthia Ross Friedman, Heidi E. K. Huttunen-Hennelly |
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| Rok vydání: | 2011 |
| Předmět: |
Magnetic Resonance Spectroscopy
Antimicrobial peptides Peptide Microbial Sensitivity Tests Microscopy Electron Transmission medicine Pharmacology (medical) Mechanisms of Action: Physiological Effects Pharmacology chemistry.chemical_classification biology Circular Dichroism Immunogold labelling medicine.disease biology.organism_classification Antimicrobial Immunohistochemistry Hemolysis Infectious Diseases Mechanism of action Biochemistry chemistry Glycine medicine.symptom Bacteria Antimicrobial Cationic Peptides |
| Zdroj: | Antimicrobial Agents and Chemotherapy. 55:2137-2145 |
| ISSN: | 1098-6596 0066-4804 |
| DOI: | 10.1128/aac.01148-10 |
| Popis: | In light of the era of microbial drug resistance, the current study aimed to better understand the relationships between sequence, higher-order structure, and mechanism of action for five designed peptides against multidrug-resistant (MDR) pathogens. All peptides studied were 15 residues long, were polycationic, adopted alpha-helical structures within hydrophobic environments (excluding the d -amino acid-substituted peptide MA-d), and contained N-terminal glycine residues, a novel antimicrobial peptide (AMP) design principle. Increasing hydrophobicity enhanced MICs (≤500 μg/ml to ≤7.4 μg/ml) without significantly increasing hemolytic activity (18% maximum hemolysis at 3,400 μg/ml). To the best of our knowledge, this is the first study to have successfully adapted and used a transmission electron microscopy (TEM) immunogold method to investigate the mechanism of action of short (∼15 residues long) AMPs within bacteria. We propose a “floodgate” mechanism to possibly explain membrane deformation and the relative absence of membrane-associated peptides 10 h into incubation. |
| Databáze: | OpenAIRE |
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