Abstract
We here report an original approach to elucidate mechanisms of action of antimicrobial peptides and derive crucial structural requirements for the design of novel therapeutic agents. The high resolution structure of TB_KKG6A, an antimicrobial peptide designed to amplify the spectrum of action of Temporin B, bound to E. coli is here determined by means of CD and NMR methodologies. We have also defined, through STD analysis, the residues in closer proximity to the bacterial membrane.
Publication types
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Letter
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Research Support, Non-U.S. Gov't
MeSH terms
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Antimicrobial Cationic Peptides / chemistry*
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Antimicrobial Cationic Peptides / metabolism
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Antimicrobial Cationic Peptides / pharmacology
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Cell Membrane / chemistry
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Cell Membrane / metabolism
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Circular Dichroism
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Drug Design
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Escherichia coli / chemistry
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Escherichia coli / metabolism
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Gram-Negative Bacteria / drug effects
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Magnetic Resonance Spectroscopy
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Protein Conformation
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Protein Structure, Tertiary
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Proteins / chemistry*
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Proteins / pharmacology
Substances
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Antimicrobial Cationic Peptides
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Proteins
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temporin