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Role of membranes in the activities of antimicrobial cationic peptides.
TLDR
A large number of cationic amphiphilic peptides found throughout nature have very broad-spectrum activities against microbes, and these peptides can traverse intact membranes to interact with internal targets.
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Interaction of Cationic Antimicrobial Peptides with Model Membranes*
TLDR
Overall, whereas all studied cationic antimicrobial peptides interacted with membranes, they were quite heterogeneous in their impact on these membranes.
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Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles.
TLDR
The structure of indolicidin bound to DPC and anionic sodium dodecyl sulfate micelles was determined using NMR methods and shown to represent a unique membrane-associated peptide structure.
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Structure and Mechanism of Action of an Indolicidin Peptide Derivative with Improved Activity against Gram-positive Bacteria*
TLDR
A cationic peptide with a unique structure and an ability to interact with membranes and to affect intracellular synthesis of proteins, RNA, and DNA is introduced.
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Interaction and Cellular Localization of the Human Host Defense Peptide LL-37 with Lung Epithelial Cells
TLDR
The results indicate the mode of interaction of LL-37 with epithelial cells and further the understanding of its role in modulating the innate immune response.
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Structural transitions as determinants of the action of the calcium-dependent antibiotic daptomycin.
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Structure-based design of an indolicidin peptide analogue with increased protease stability.
TLDR
It is suggested that cyclization may serve as an important strategy in the rational design of antimicrobial peptides.
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A novel approach for emerging and antibiotic resistant infections: Innate defense regulators as an agnostic therapy.
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Membrane binding and permeation by indolicidin analogs studied by a biomimetic lipid/polydiacetylene vesicle assay
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Structure-activity relationships for the beta-hairpin cationic antimicrobial peptide polyphemusin I.
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