| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1938347 | Biochemical and Biophysical Research Communications | 2007 | 7 Pages |
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 α-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.
Keywords
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
César Segura, Fanny Guzmán, Luz Mary Salazar, Manuel E. Patarroyo, Sergio Orduz, Victor Lemeshko,