Separate, lower-density inclusions containing the D13 scaffold protein and endoplasmic reticulum membranes were also present. These features are most similar to those previously seen when expression of A11, another conserved nonvirion protein, is repressed.”
“Introduction: A variety of (bis)thiosemicarbazone-based ligand systems have been investigated as chelating agents for Au(III) complexes with potential radiotherapeutic applications. Ligand systems containing an ethyl, propyl or butyl backbone between the two imine N donors have been synthesized to evaluate chelate ring size effects on the resultant Au(Ill) complex stability at the macroscopic and radiotracer
levels.
Methods: The Au(III) complexes were synthesized and characterized by NMR, electrospray Selleck Mdivi1 ionization mass spectra, elemental analysis and X-ray crystallography. The (198)Au complexes were evaluated in vitro at the tracer level for stability in phosphate-buffered
saline at pH 7.4 and 37 degrees C. One of these complexes [(198)Au(3,4-HxTSE)] showed high in vitro stability and was further evaluated in vivo in normal mice.
Results: [Au(ATSM)]AUCl(4)center dot 2CH(3)OH, (ATSM=diacetyl-bis(N(4)-methylthiosemicarbazone)) H(14)C(8)N(6)O(2)S(2)Cl(4)Au(2)center dot 2CH(3)OH, crystallized from methanol in the monoclinic space group P21/n with a=14.7293(13) angstrom, b=7.7432(7) PI3K inhibitor angstrom, c=20.4363(18) angstrom, beta=100.140(2)degrees, V=2294.4 (4) angstrom(3), Z=4; [Au(3,4-HxTSE)]Cl center dot CH(3)CH(2)OH/AuCl(2), (3,4-HxTSE=3,4-hexanedione-bis(N(4)-ethylthiosemicarbazone)) H(26)C(13.6)N(6)O(0.8)S(2)Cl(1.2)Au(1.2), crystallized from ethanol in the monoclinic space group P21/c with a=10.1990(10) angstrom, b=13.8833(14) Org 27569 angstrom, c=15.1752(15) angstrom, beta=99.353(2)degrees, V=2120.2 (4) angstrom, Z=4.
Conclusions: These studies revealed poor stability of the [(198)Au][Au(3,4-HxTSE)](+) complex; however, crystal structure data suggest potential alterations to the ligand backbone may increase stability.
(C) 2010 Elsevier Inc. All rights reserved.”
“The membrane-proximal external region (MPER) of the human immunodeficiency virus (HIV) envelope glycoprotein (gp41) is critical for viral fusion and infectivity and is the target of three of the five known broadly neutralizing HIV type 1 (HIV-1) antibodies, 2F5, Z13, and 4E10. Here, we report the crystal structure of the Fab fragment of Z13e1, an affinity-enhanced variant of monoclonal antibody Z13, in complex with a 12-residue peptide corresponding to the core epitope (W(670)NWFDITN(677)) at 1.8-angstrom resolution. The bound peptide adopts an S-shaped conformation composed of two tandem, perpendicular helical turns. This conformation differs strikingly from the alpha-helical structure adopted by an overlapping MPER peptide bound to 4E10.