8b4s

Antimicrobial peptide capitellacin from polychaeta Capitella teleta in DPC (dodecylphosphocholine) micelles, dimeric form

spinqualitylabelsall models 8b4s Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8b4s is a 2 chain structure with sequence from Capitella teleta. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 20 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function R7TSD6_CAPTE Publication Abstract from PubMed Capitellacin is the beta-hairpin membrane-active cationic antimicrobial peptide from the marine polychaeta Capitella teleta. Capitellacin exhibits antibacterial activity, including against drug-resistant strains. To gain insight into the mechanism of capitellacin action, we investigated the structure of the peptide in the membrane-mimicking environment of dodecylphosphocholine (DPC) micelles using high-resolution NMR spectroscopy. In DPC solution, two structural forms of capitellacin were observed: a monomeric beta-hairpin was in equilibrium with a dimer formed by the antiparallel association of the N-terminal beta-strands and stabilized by intermonomer hydrogen bonds and Van der Waals interactions. The thermodynamics of the enthalpy-driven dimerization process was studied by varying the temperature and molar ratios of the peptide to detergent. Cooling the peptide/detergent system promoted capitellacin dimerization. Paramagnetic relaxation enhancement induced by lipid-soluble 12-doxylstearate showed that monomeric and dimeric capitellacin interacted with the surface of the micelle and did not penetrate into the micelle interior, which is consistent with the "carpet" mode of membrane activity. An analysis of the known structures of beta-hairpin AMP dimers showed that their dimerization in a membrane-like environment occurs through the association of polar or weakly hydrophobic surfaces. A comparative analysis of the physicochemical properties of beta-hairpin AMPs revealed that dimer stability and hemolytic activity are positively correlated with surface hydrophobicity. An additional positive correlation was observed between hemolytic activity and AMP charge. The data obtained allowed for the provision of a more accurate description of the mechanism of the oligomerization of beta-structural peptides in biological membranes. Dimerization of the beta-Hairpin Membrane-Active Cationic Antimicrobial Peptide Capitellacin from Marine Polychaeta: An NMR Structural and Thermodynamic Study.,Mironov PA, Paramonov AS, Reznikova OV, Safronova VN, Panteleev PV, Bolosov IA, Ovchinnikova TV, Shenkarev ZO Biomolecules. 2024 Mar 11;14(3):332. doi: 10.3390/biom14030332. PMID:38540752 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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