Abstract
The cell membrane is the first barrier and quite often the primary target that antimicrobial peptides (AMPs) have to destroy or penetrate to fulfill their mission. Upon penetrating through the membrane, the peptides can further attack intracellular targets, in particular DNA. Studying the interaction of an antimicrobial peptide with a cell membrane and DNA holds keys to understanding its killing mechanisms. Commonly, these interactions are studied by using optical or scanning electron microscopy and appropriately labeled peptides. However, labeling can significantly affect the hydrophobicity, conformation, and size of the peptide, hence altering the interaction significantly. Here, we describe the use of atomic force microscopy (AFM) for a label-free study of the interactions of peptides with model membranes under physiological conditions and DNA as a possible intracellular target.
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Acknowledgments
This work was generously supported by grants from the Spar Nord Foundation and the Det Obelske Familiefond. The authors also acknowledge fruitful discussions with Patrick Markus.
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Fojan, P., Gurevich, L. (2017). Atomic Force Microscopy Study of the Interactions of Indolicidin with Model Membranes and DNA. In: Hansen, P. (eds) Antimicrobial Peptides. Methods in Molecular Biology, vol 1548. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-6737-7_14
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DOI: https://doi.org/10.1007/978-1-4939-6737-7_14
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