Cargando…
Minor sequence modifications in temporin B cause drastic changes in antibacterial potency and selectivity by fundamentally altering membrane activity
Antimicrobial peptides (AMPs) are a potential source of new molecules to counter the increase in antimicrobial resistant infections but a better understanding of their properties is required to understand their native function and for effective translation as therapeutics. Details of the mechanism o...
Autores principales: | Manzo, Giorgia, Ferguson, Philip M., Gustilo, V. Benjamin, Hind, Charlotte K., Clifford, Melanie, Bui, Tam T., Drake, Alex F., Atkinson, R. Andrew, Sutton, J. Mark, Batoni, Giovanna, Lorenz, Christian D., Phoenix, David A., Mason, A. James |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6362004/ https://www.ncbi.nlm.nih.gov/pubmed/30718667 http://dx.doi.org/10.1038/s41598-018-37630-3 |
Ejemplares similares
-
Temporin L and aurein 2.5 have identical conformations but subtly distinct membrane and antibacterial activities
por: Manzo, Giorgia, et al.
Publicado: (2019) -
Temporin B Forms Hetero-Oligomers with Temporin L,
Modifies Its Membrane Activity, and Increases the Cooperativity of
Its Antibacterial Pharmacodynamic Profile
por: Ferguson, Philip M., et al.
Publicado: (2022) -
A pleurocidin analogue with greater conformational flexibility, enhanced antimicrobial potency and in vivo therapeutic efficacy
por: Manzo, Giorgia, et al.
Publicado: (2020) -
Synergistic Antibacterial and Anti-Inflammatory Activity of Temporin A and Modified Temporin B In Vivo
por: Capparelli, Rosanna, et al.
Publicado: (2009) -
Antimicrobial Peptide Potency is Facilitated by Greater Conformational Flexibility when Binding to Gram-negative Bacterial Inner Membranes
por: Amos, Sarah-Beth T. A., et al.
Publicado: (2016)