5nf0 | pdb_00005nf0

Discovery, crystal structures and atomic force microscopy study of thioether ligated D,L-cyclic antimicrobial peptides against multidrug resistant Pseudomonas aeruginosa

spinqualitylabelsall models 5nf0, resolution 1.27Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5nf0 is a 8 chain structure with sequence from Pseudomonas aeruginosa and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.271Å Ligands: CA, DCY, DLY, DTR, NH2, OXE, ZDC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9HYN5_PSEAE Publication Abstract from PubMed Here we report a new family of cyclic antimicrobial peptides (CAMPs) targeting MDR strains of Pseudomonas aeruginosa. These CAMPs are cyclized via a xylene double thioether bridge connecting two cysteines placed at the ends of a linear amphiphilic alternating d,l-sequence composed of lysines and tryptophans. Investigations by transmission electron microscopy (TEM), dynamic light scattering and atomic force microscopy (AFM) suggest that these peptide macrocycles interact with the membrane to form lipid-peptide aggregates. Amphiphilic conformations compatible with membrane disruption are observed in high resolution X-ray crystal structures of fucosylated derivatives in complex with lectin LecB. The potential for optimization is highlighted by N-methylation of backbone amides leading to derivatives with similar antimicrobial activity but lower hemolysis. Design, crystal structure and atomic force microscopy study of thioether ligated d,l-cyclic antimicrobial peptides against multidrug resistant Pseudomonas aeruginosa.,He R, Di Bonaventura I, Visini R, Gan BH, Fu Y, Probst D, Luscher A, Kohler T, van Delden C, Stocker A, Hong W, Darbre T, Reymond JL Chem Sci. 2017 Nov 1;8(11):7464-7475. doi: 10.1039/c7sc01599b. Epub 2017 Sep 4. PMID:29163899 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA