Effects of RAMEA-complexed polyunsaturated fatty acids on the response of human dendritic cells to inflammatory signals

• Éva Rajnavölgyi,
• Renáta Laczik,
• Viktor Kun,
• Lajos Szente and
• Éva Fenyvesi

Beilstein J. Org. Chem. 2014, 10, 3152–3160, doi:10.3762/bjoc.10.332

• moDC differentiation and activation by using flow cytometry. Monocyte-derived DC activation was also monitored by the secretion level of the pro- and anti-inflammatory cytokines IL-1β, TNF-α, IL-6, IL-10 and IL-12, respectively. We found that RAMEA-complexed n−3 fatty acids reduced the expression of

• mediated through the GP120 receptor without interfering with the cell membrane structure. Keywords: cell membrane; cell surface markers; cyclodextrin; enzyme immunoassay; flow cytometry; monocyte-derived dendritic cells; proinflammatory cytokines; RAMEA; solubilization; Introduction The n−3

• moDC were stimulated with LPS or Poly(I:C) mimicking bacterial and viral infections, respectively or were left untreated and the response of unstimulated and activated moDC was monitored by measuring the expression levels of CD1a and the DC activation marker CD83 by flow cytometry. CD83 was selected

Human dendritic cell activation induced by a permannosylated dendron containing an antigenic GM₃-lactone mimetic

• Renato Ribeiro-Viana,
• Elena Bonechi,
• Javier Rojo,
• Clara Ballerini,
• Giuseppina Comito,
• Barbara Richichi and
• Cristina Nativi

Beilstein J. Org. Chem. 2014, 10, 1317–1324, doi:10.3762/bjoc.10.133

• incubation with LPS (1 µg/mL, Sigma–Aldrich), compound 5 and scaffold 7 (two doses, 50 and 10 µg/mL). DC phenotype The DC phenotype was analyzed by flow cytometry with a 4 color EpicsXL cytometer (Beckman–Coulter), equipped with Expo 32 software. Cell surface markers were labelled with monoclonal antibodies

Synthesis and evaluation of cell-permeable biotinylated PU-H71 derivatives as tumor Hsp90 probes

• Tony Taldone,
• Anna Rodina,
• Erica M. DaGama Gomes,
• Matthew Riolo,
• Hardik J. Patel,
• Raul Alonso-Sabadell,
• Danuta Zatorska,
• Maulik R. Patel,
• Sarah Kishinevsky and
• Gabriela Chiosis

Beilstein J. Org. Chem. 2013, 9, 544–556, doi:10.3762/bjoc.9.60

• and, as we show, represents a unique and useful tool to probe tumor Hsp90 biology in live cells by affinity capture, flow cytometry and confocal microscopy. To our knowledge, 2g is the only reported biotinylated Hsp90 probe to have such combined characteristics. Keywords: affinity capture; biotin

• ; flow cytometry; fluorescence microscopy; PU-H71; tumor Hsp90; Introduction Heat shock protein 90 (Hsp90) is a molecular chaperone that functions to properly fold proteins to their active conformation through its ATPase activity [1]. These client proteins include many that are involved in malignant

• cell homogenates, these compounds may be further used to investigate Hsp90 complexes in live cells, which represents a more physiologically relevant state. These tools also have use in flow cytometry and microscopy, whereby fluorescently labeled antibodies to biotin are used, as we describe below

Dimerization of a cell-penetrating peptide leads to enhanced cellular uptake and drug delivery

• Jan Hoyer,
• Ulrich Schatzschneider,
• Michaela Schulz-Siegmund and
• Ines Neundorf

Beilstein J. Org. Chem. 2012, 8, 1788–1797, doi:10.3762/bjoc.8.204

• a dramatically improved capacity to internalize into various cell lines, even primary cells, using flow cytometry and fluorescence microscopy. Cell viability assays indicated increased cytotoxicity of the dimer presumably caused by membrane leakage; however, this effect turned out to be dependent on

• ) were grown in DMEM high glucose (4.5 g/L) containing 1% penicillin/streptomycin and 10% FBS. Internalization studies For peptide-uptake studies by flow cytometry, cells were seeded in a 48-well plate and grown to 60–70% confluence. After incubation at 37 °C for 1 h with 5(6)-carboxyfluorescein-labeled