| Literature DB >> 28013506 |
Peter Fojan1, Leonid Gurevich2.
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.Entities:
Keywords: Antimicrobial peptides (AMPs); Atomic force microscopy (AFM); Indolicidin; Peptide–DNA interaction; Supported planar bilayers (SPBs)
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Year: 2017 PMID: 28013506 DOI: 10.1007/978-1-4939-6737-7_14
Source DB: PubMed Journal: Methods Mol Biol ISSN: 1064-3745