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PubMed · 17207468

BTM-P1 polycationic peptide biological activity and 3D-dimensional structure.

César Segura·Fanny Guzmán·Luz Mary Salazar·Manuel E Patarroyo·Sergio Orduz·Victor Lemeshko
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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.

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Amino Acid SequenceAnimalsAntimicrobial Cationic PeptidesBacteriaBacterial ProteinsBacterial ToxinsCircular DichroismIonophoresMaleMitochondrial MembranesMitochondrial ProteinsMitochondrial SwellingModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularProtein ConformationProtein Structure, SecondaryRatsJournal ArticleResearch Support, Non-U.S. Gov't

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César Segura, Fanny Guzmán, Luz Mary Salazar, Manuel E Patarroyo, Sergio Orduz, Victor Lemeshko. 2006-12-22. BTM-P1 polycationic peptide biological activity and 3D-dimensional structure.. https://doi.org/10.1016/j.bbrc.2006.12.113

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