Abstract
The novel BTM-P1 peptide interferes with energetic processes in mitochondria; its antimicrobial activity against Gram-positive and Gram-negative bacteria is described here. BTM-P1 three-dimensional structure was determined by 1H NMR to explain its biological mechanisms and membrane activity. Structural data indicated that BTM-P1 can form an alpha-helix; circular dichroism analysis confirmed the peptide's propensity to behave as a typical transmembrane helix in a lipidic environment. According to the structural characteristics of the polycationic BTM-P1 peptide so revealed, its biological activity can be explained by a mechanism involving the formation of ion-permeable channels in biomembranes.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Antimicrobial Cationic Peptides / chemistry*
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Antimicrobial Cationic Peptides / isolation & purification
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Antimicrobial Cationic Peptides / pharmacology*
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Bacteria / drug effects*
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Bacteria / growth & development
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Bacterial Proteins / pharmacology
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Bacterial Toxins / pharmacology
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Circular Dichroism
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Ionophores / pharmacology
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Male
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Mitochondrial Membranes / drug effects
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Mitochondrial Proteins / chemistry
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Mitochondrial Proteins / isolation & purification
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Mitochondrial Proteins / pharmacology
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Mitochondrial Swelling / drug effects
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Models, Molecular
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Molecular Sequence Data
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Nuclear Magnetic Resonance, Biomolecular
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Protein Conformation
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Protein Structure, Secondary
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Rats
Substances
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Antimicrobial Cationic Peptides
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BTM-P1 peptide
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Bacterial Proteins
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Bacterial Toxins
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CRY11BB protein, Bacillus thuringiensis
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Ionophores
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Mitochondrial Proteins