TY - JOUR A1 - Paulus, Florian A1 - Weiss, Maximilian A1 - Steinhilber, Dirk A1 - Nikitin, Anatoly A1 - Schütte, Christof A1 - Haag, Rainer T1 - Anionic Ring-Opening Polymerization Simulations for Hyperbranched Polyglycerols with Defined Molecular Weights JF - Macromolecules Y1 - 2013 U6 - https://doi.org/10.1021/ma401712w VL - 46 IS - 21 SP - 8458 EP - 8466 ER - TY - JOUR A1 - Weber, Marcus A1 - Bujotzek, Alexander A1 - Andrae, Karsten A1 - Weinhart, M. A1 - Haag, Rainer T1 - Computational entropy estimation of linear polyether modified surfaces and correlation with protein resistant properties of such surfaces JF - J. Mol. Sim. Y1 - 2011 ER - TY - JOUR A1 - Weber, Marcus A1 - Bujotzek, Alexander A1 - Haag, Rainer T1 - Quantifying the rebinding effect in multivalent chemical ligand-receptor systems JF - J. Chem. Phys. Y1 - 2012 VL - 137 IS - 5 SP - 054111 ER - TY - JOUR A1 - Fasting, Carlo A1 - Schalley, Christoph A. A1 - Weber, Marcus A1 - Seitz, Oliver A1 - Hecht, Stefan A1 - Koksch, Beate A1 - Dernedde, Jens A1 - Graf, Christina A1 - Knapp, Ernst-Walter A1 - Haag, Rainer T1 - Multivalency as a Chemical Organization and Action Principle JF - Angew. Chem. Int. Ed. Y1 - 2012 VL - 51 IS - 42 SP - 10472 EP - 10498 ER - TY - JOUR A1 - Weiss, Maximilian A1 - Paulus, Florian A1 - Steinhilber, D. A1 - Nikitin, Anatoly A1 - Haag, Rainer A1 - Schütte, Christof T1 - Estimating Kinetic Parameters for the Spontaneous Polymerization of Glycidol at Elevated Temperatures JF - MACROMOLECULAR THEORY and SIMULATIONS Y1 - 2012 UR - http://publications.imp.fu-berlin.de/1142/ U6 - https://doi.org/10.1002/mats.201200003 VL - 21 IS - 7 SP - 470 EP - 481 ER - TY - JOUR A1 - Abendroth, Frank A1 - Bujotzek, Alexander A1 - Shan, Min A1 - Haag, Rainer A1 - Weber, Marcus A1 - Seitz, Oliver T1 - DNA-controlled bivalent presentation of ligands for the estrogen receptor JF - Angew. Chem. Int. Ed. Y1 - 2011 ER - TY - JOUR A1 - Bujotzek, Alexander A1 - Shan, Min A1 - Haag, Rainer A1 - Weber, Marcus T1 - Towards a rational spacer design for bivalent inhibition of estrogen receptor JF - J. Comput.-Aided Mol. Des. Y1 - 2011 VL - 25(3) SP - 253 EP - 262 ER - TY - JOUR A1 - Koschek, A1 - Durmaz, Vedat A1 - Krylova, A1 - Wieczorek, A1 - Gupta, Pooja A1 - Richter, A1 - Bujotzek, Alexander A1 - Fischer, A1 - Haag, Rainer A1 - Freund, A1 - Weber, Marcus A1 - Rademann, T1 - Peptide polymer ligands for a tandem WW-domain, a soft multivalent protein-protein interaction: lessons on the thermodynamic fitness of flexible ligands JF - Beilstein J. Org. Chem. Y1 - 2015 VL - 11 SP - 837 EP - 847 ER - TY - JOUR A1 - Weber, Marcus A1 - Zoschke, Christian A1 - Sedighi, Amir A1 - Fleige, Emanuel A1 - Haag, Rainer A1 - Schäfer-Korting, Monika T1 - Free Energy Simulations of Drug loading for Core-Multishell Nanotransporters JF - J Nanomed Nanotechnol Y1 - 2014 U6 - https://doi.org/10.4172/2157-7439.1000234 VL - 5 IS - 5 SP - 234 ER - TY - JOUR A1 - Tyagi, Rahul A1 - Malhotra, Shashwat A1 - Thünemann, Andreas F. A1 - Sedighi, Amir A1 - Weber, Marcus A1 - Schäfer, Andreas A1 - Haag, Rainer T1 - Investigations of Host-Guest Interactions with Shape-persistent Nonionic Dendritic Micelles JF - J. Phys. Chem. C Y1 - 2013 VL - 117 IS - 23 SP - 12307 EP - 12317 ER - TY - JOUR A1 - Shan, Min A1 - Carlson, Kathryn E. A1 - Bujotzek, Alexander A1 - Wellner, Anja A1 - Gust, Ronald A1 - Weber, Marcus A1 - Katzenellenbogen, John A. A1 - Haag, Rainer T1 - Nonsteroidal Bivalent Estrogen Ligands - An Application of the Bivalent Concept to the Estrogen Receptor JF - ACS Chem. Biol. Y1 - 2013 VL - 8 IS - 4 SP - 707 EP - 715 ER - TY - JOUR A1 - Shan, Min A1 - Bujotzek, Alexander A1 - Abendroth, Frank A1 - Seitz, Oliver A1 - Weber, Marcus A1 - Haag, Rainer T1 - Conformational Analysis of Bivalent Estrogen Receptor-Ligands: From Intramolecular to Intermolecular Binding JF - ChemBioChem, 12(17) Y1 - 2011 U6 - https://doi.org/10.1002/cbic.201100529 SP - 2587 EP - 2598 ER - TY - JOUR A1 - Fricke, Mackenzie S. A1 - Frometa, Magalee R. A1 - Kerkhoff, Yannic A1 - Bernhard, Samuel P. A1 - Tahir, Ramat S. A1 - Quaas, Elisa A1 - Totten, William H. A1 - Haag, Rainer A1 - Achazi, Katharina A1 - Cloninger, Mary J. T1 - The toxicity, uptake, and impact on galectin-3 mediated apoptosis of lactose functionalized PAMAM dendrimers JF - Materials Advances N2 - Poly(amidoamine) (PAMAM) dendrimers functionalized with ligands that are designed to interact with biological receptors are important macromolecules for the elucidation and mediation of biological recognition processes. Specifically, carbohydrate functionalized dendrimers are useful synthetic multivalent systems for the study of multivalent protein–carbohydrate interactions. For example, lactose functionalized glycodendrimers can be used to discern the function of galectins, galactoside-binding proteins that are often over-expressed during cancer progression. In order to effectively interpret cancer cellular assays using glycodendrimers, however, their properties in the presence of cells must first be assessed. Macromolecules that are taken up by cells would be expected to have access to many different cell signaling pathways and modes of action that solely extracellular macromolecules cannot utilize. In addition, macromolecules that display cellular toxicity could not be used as drug delivery vehicles. Here, we report fundamental studies of cellular toxicity, viability, and uptake with four generations of lactose functionalized PAMAM dendrimers. In all cases, the dendrimers are readily taken up by the cells but do not display any significant cellular toxicity. The glycodendrimers also increase cellular apoptosis, suggesting that they may abrogate the antiapoptotic protections afforded by galectin-3 to cancer cells. The results reported here indicate that appropriately functionalized PAMAM dendrimers can be used as nontoxic tools for the study and mediation of both extra and intracellular cancer processes. Y1 - 2025 U6 - https://doi.org/10.1039/D4MA00782D VL - 6 SP - 3171 EP - 3184 ER - TY - JOUR A1 - Khatri, Vinod A1 - Boback, Nico A1 - Abdelwahab, Hassan A1 - Niemeyer, Daniela A1 - Palmer, Tahlia M. A1 - Sahoo, Anil Kumar A1 - Kerkhoff, Yannic A1 - Ludwig, Kai A1 - Balci, Dilara A1 - Trimpert, Jakob A1 - Haag, Rainer A1 - Povolotsky, Tatyana L. A1 - Netz, Roland R. A1 - Drosten, Christian A1 - Lauster, Daniel C. A1 - Bhatia, Sumati T1 - Polysialosides outperform sulfated analogs for the inhibition of SARS-CoV-2 JF - Small N2 - Both polysialosides and polysulfates are known to interact with the receptor binding domain (RBD) of the SARS-CoV-2 spike protein. However, a comprehensive site by site analysis of their binding affinities and potential synergistic antiviral effects have not been performed. Here, we report on the synthesis of polysialosides with nanomolar binding affinities to spike proteins of SARS-CoV-2 in solution using microscale thermophoresis (MST). The dendritic polyglycerol based polysialosides dPG500(SA)0.55 and dPG500(SA)0.25, with a dissociation constant Kd of 4.78 nM and 10.85 nM, respectively, bind ~500 times stronger than the high density polysulfated analog dPG500(OSO3Na)0.55, to intact SARS-CoV-2 virus particles or isolated spike protein. In fact, the presence of sulfate groups in a heteromultivalent compound dPG500(SA)0.20(OSO3Na)0.20 weakens the binding to spike proteins. A polycarboxylated analog does not bind to SARS-CoV-2, ruling out that the interaction of polysialoside is simply driven by electrostatic interactions. Furthermore, we found potent nanomolar binding of dPG500(SA)0.55 to SARS-CoV-2 variant B.1.617 (Delta) and B.1.1.529 (Omicron) RBD. Using explicit-solvent all-atom molecular dynamics (MD) simulations and docking studies, we obtain atomistic details on the interaction of different functional groups with the SARS-CoV-2 RBD and their binding affinities. Our data support the conclusion that sialosides interact stronger with RBD than sulfates. Notably, our most affine binder dPG500(SA)0.55 inhibits SARS-CoV-2 (WT, D614G) replication up to 98.6% at low nanomolar concentrations. Y1 - 2025 UR - https://doi.org/10.26434/chemrxiv-2024-8b0gb U6 - https://doi.org/10.1002/smll.202500719 VL - 21 IS - 34 ER - TY - JOUR A1 - Lang, Annemarie A1 - Helfmeier, Sarah A1 - Stefanowski, Jonathan A1 - Kuppe, Aditi A1 - Sunkara, Vikram A1 - Pfeiffenberger, Moritz A1 - Wolter, Angelique A1 - Damerau, Alexandra A1 - Hemmati-Sadeghi, Shabnam A1 - Ringe, Jochen A1 - Haag, Rainer A1 - Hauser, Anja E. A1 - Löhning, Max A1 - Perka, Carsten A1 - Duda, Georg A1 - Hoff, Paula A1 - Schmidt-Bleek, Katharina A1 - Gaber, Timo A1 - Buttgereit, Frank T1 - HIF-stabilization prevents delayed fracture healing JF - bioarxiv Y1 - 2020 U6 - https://doi.org/10.1101/2020.07.02.182832 ER -