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Blood eosinophils in COPD: friend or foe?. Anastasia Papaporfyriou, Petros Bakakos, Georgios Hillas, Andriana I.International Journal of Molecular Sciences 2022, 23 Antimicrobial Peptide Mechanisms Studied by Whole-Cell Deuterium NMR. Bactericidal Activity Engineered on Human Pancreatic Ribonuclease and Onconase. Gerard Torrent, Marc Ribó, Antoni Benito and Maria Vilanova.Binding of Functionalized Paramagnetic Nanoparticles to Bacterial Lipopolysaccharides And DNA. Chang, Carmen Alvarez-Lorenzo, Beatriz Magariños, Angel Concheiro and T. Eosinophil Cationic Protein Aggregation: Identification of an N-Terminus Amyloid Prone Region. Refining the Eosinophil Cationic Protein Antibacterial Pharmacophore by Rational Structure Minimization. Victòria Nogués, Marta Bruix, David Andreu, and Ester Boix. Marc Torrent, David Pulido, Beatriz G.Understanding the Dark and Light-Enhanced Bactericidal Action of Cationic Conjugated Polyelectrolytes and Oligomers. Designing Cell-Aggregating Peptides without Cytotoxicity. ACS Applied Materials & Interfaces 2017, 9 Structure–Activity Relationship of Membrane-Targeting Cationic Ligands on a Silver Nanoparticle Surface in an Antibiotic-Resistant Antibacterial and Antibiofilm Activity Assay. Xiaomei Dai, Xuelei Chen, Jing Zhao, Yu Zhao, Qianqian Guo, Tianqi Zhang, Chunli Chu, Xinge Zhang, and Chaoxing Li.Enhanced Antibacterial Properties of Self-Assembling Peptide Amphiphiles Functionalized with Heparin-Binding Cardin-Motifs. Run Chang, Keerthana Subramanian, Mian Wang, and Thomas J.Solid-State NMR Investigations of Extracellular Matrixes and Cell Walls of Algae, Bacteria, Fungi, and Plants. Nader Ghassemi, Alexandre Poulhazan, Fabien Deligey, Frederic Mentink-Vigier, Isabelle Marcotte, Tuo Wang.This article is cited by 92 publications. The protein binding to the bacteria-wall surface would represent a first encounter step key in its antimicrobial mechanism of action. coli does not require any pretreatment to overcome the outer membrane barrier. Moreover, the depolarization activity on E. ECP also activates the cytoplasmic membrane depolarization in both strains. Although both bacteria strain cells retain their shape and no cell lysis is patent, the protein can induce in E. The protein damages the bacteria surface and induces the cell population aggregation on E. Ultrastructural analysis of cell bacteria wall and morphology have been visualized by scanning and transmission electron microscopy in both Escherichia coli and Staphylococcus aureus strains. The protein also binds in vivo to bacteria cells. ECP high-affinity binding capacity to LPSs and lipid A has been analyzed by a fluorescent displacement assay, and the corresponding dissociation constants were calculated using the protein labeled with a fluorophor. We have analyzed its specific association to lipopolysaccharides (LPSs), its lipid A component, and peptidoglycans (PGNs). We have now shown that ECP can bind with high affinity to the bacteria-wall components. The protein can destabilize lipid bilayers, although the action at the membrane level can only partially account for its bactericidal activity. The protein displays antimicrobial activity against both Gram-negative and Gram-positive strains. The eosinophil cationic protein (ECP) is an eosinophil-secreted RNase involved in the immune host defense, with a cytotoxic activity against a wide range of pathogens.