| Literature DB >> 17207468 |
César Segura1, Fanny Guzmán, Luz Mary Salazar, Manuel E Patarroyo, Sergio Orduz, Victor Lemeshko.
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.Entities:
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Year: 2006 PMID： 17207468 DOI： 10.1016/j.bbrc.2006.12.113
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575