BTM-P1 polycationic peptide biological activity and 3D-dimensional structure.
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.
Segura
César
C
Grupo Malaria, Sede de Investigación Universitaria, Universidad de Antioquia, Medellín, Colombia.
Guzmán
Fanny
F
Salazar
Luz Mary
LM
Patarroyo
Manuel E
ME
Orduz
Sergio
S
Lemeshko
Victor
V
D000595:Amino Acid Sequence; D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology*; D001419:Bacteria / Q000187:drug effects* / Q000254:growth & development; D001426:Bacterial Proteins / Q000494:pharmacology; D001427:Bacterial Toxins / Q000494:pharmacology; D002942:Circular Dichroism; D007476:Ionophores / Q000494:pharmacology; D008297:Male; D051336:Mitochondrial Membranes / Q000187:drug effects; D024101:Mitochondrial Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology; D008933:Mitochondrial Swelling / Q000187:drug effects; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D051381:Rats
D023181:Antimicrobial Cationic Peptides; C501422:BTM-P1 peptide; D001426:Bacterial Proteins; D001427:Bacterial Toxins; C115468:CRY11BB protein, Bacillus thuringiensis; D007476:Ionophores; D024101:Mitochondrial Proteins