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Título

Antimicrobial peptides: To membranes and beyond

AutorMarcos López, José Francisco ; Gandía Gómez, Mónica
Palabras claveAntibacterial peptide
Antifungal peptide
Antimicrobial mechanism
Apoptosis
Cell-penetrating peptides
Chaperone
Glycan
MAPK signaling
Membrane permeation
Two-component system
Fecha de publicaciónjun-2009
EditorTaylor & Francis
CitaciónExpert Opinion on Drug Discovery 4(6): 659-671 (2009)
Resumen[Background] Antimicrobial peptides (AMP) are widely recognized as promising alternatives to the current use of antibiotics and fungicides. Amino acid sequences of a vast majority of AMP share cationic and amphipathic biophysical properties that allow their insertion into lipid bilayers, and can lead to alteration of biological membrane functions. Initial characterization studies linked these properties to antimicrobial killing activity. However, additional data indicate that this is not the sole mode of action and that more subtle mechanisms might mediate the interaction with and effect to target microbes, as well as the specificity and toxicity of peptides. As such, antimicrobial peptides are increasingly viewed as powerful multifunctional drugs.
[Objective] This review will summarize findings on these alternative non-lytic modes of antimicrobial action that go beyond membrane disruption, with an emphasis on the specific interaction with microbial cell wall/membrane components, signaling of AMP exposure, and intracellular targets of peptide characterize and exploit these antimicrobial properties.
[Conclusion] Detailed knowledge on non-lytic modes of action of antimicrobial peptides will help in the design and discovery of novel antibacterial and antifungal compounds.
Descripción13 pages, 1 figures, 2 tables.
Versión del editorhttp://dx.doi.org/10.1517/17460440902992888
URIhttp://hdl.handle.net/10261/14957
DOI10.1517/17460440902992888
ISSN1746-0441
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