@article{PaulusWeissSteinhilberetal.2013, author = {Paulus, Florian and Weiss, Maximilian and Steinhilber, Dirk and Nikitin, Anatoly and Sch{\"u}tte, Christof and Haag, Rainer}, title = {Anionic Ring-Opening Polymerization Simulations for Hyperbranched Polyglycerols with Defined Molecular Weights}, volume = {46}, journal = {Macromolecules}, number = {21}, doi = {10.1021/ma401712w}, pages = {8458 -- 8466}, year = {2013}, language = {en} } @article{WeberBujotzekAndraeetal.2011, author = {Weber, Marcus and Bujotzek, Alexander and Andrae, Karsten and Weinhart, M. and Haag, Rainer}, title = {Computational entropy estimation of linear polyether modified surfaces and correlation with protein resistant properties of such surfaces}, journal = {J. Mol. Sim.}, year = {2011}, language = {en} } @article{WeberBujotzekHaag2012, author = {Weber, Marcus and Bujotzek, Alexander and Haag, Rainer}, title = {Quantifying the rebinding effect in multivalent chemical ligand-receptor systems}, volume = {137}, journal = {J. Chem. Phys.}, number = {5}, pages = {054111}, year = {2012}, language = {en} } @article{FastingSchalleyWeberetal.2012, author = {Fasting, Carlo and Schalley, Christoph A. and Weber, Marcus and Seitz, Oliver and Hecht, Stefan and Koksch, Beate and Dernedde, Jens and Graf, Christina and Knapp, Ernst-Walter and Haag, Rainer}, title = {Multivalency as a Chemical Organization and Action Principle}, volume = {51}, journal = {Angew. Chem. Int. Ed.}, number = {42}, pages = {10472 -- 10498}, year = {2012}, language = {en} } @article{WeissPaulusSteinhilberetal.2012, author = {Weiss, Maximilian and Paulus, Florian and Steinhilber, D. and Nikitin, Anatoly and Haag, Rainer and Sch{\"u}tte, Christof}, title = {Estimating Kinetic Parameters for the Spontaneous Polymerization of Glycidol at Elevated Temperatures}, volume = {21}, journal = {MACROMOLECULAR THEORY and SIMULATIONS}, number = {7}, doi = {10.1002/mats.201200003}, pages = {470 -- 481}, year = {2012}, language = {en} } @article{AbendrothBujotzekShanetal.2011, author = {Abendroth, Frank and Bujotzek, Alexander and Shan, Min and Haag, Rainer and Weber, Marcus and Seitz, Oliver}, title = {DNA-controlled bivalent presentation of ligands for the estrogen receptor}, journal = {Angew. Chem. Int. Ed.}, year = {2011}, language = {en} } @article{BujotzekShanHaagetal.2011, author = {Bujotzek, Alexander and Shan, Min and Haag, Rainer and Weber, Marcus}, title = {Towards a rational spacer design for bivalent inhibition of estrogen receptor}, volume = {25(3)}, journal = {J. Comput.-Aided Mol. Des.}, pages = {253 -- 262}, year = {2011}, language = {en} } @article{KoschekDurmazKrylovaetal.2015, author = {Koschek, and Durmaz, Vedat and Krylova, and Wieczorek, and Gupta, Pooja and Richter, and Bujotzek, Alexander and Fischer, and Haag, Rainer and Freund, and Weber, Marcus and Rademann,}, title = {Peptide polymer ligands for a tandem WW-domain, a soft multivalent protein-protein interaction: lessons on the thermodynamic fitness of flexible ligands}, volume = {11}, journal = {Beilstein J. Org. Chem.}, pages = {837 -- 847}, year = {2015}, language = {en} } @article{WeberZoschkeSedighietal.2014, author = {Weber, Marcus and Zoschke, Christian and Sedighi, Amir and Fleige, Emanuel and Haag, Rainer and Sch{\"a}fer-Korting, Monika}, title = {Free Energy Simulations of Drug loading for Core-Multishell Nanotransporters}, volume = {5}, journal = {J Nanomed Nanotechnol}, number = {5}, doi = {10.4172/2157-7439.1000234}, pages = {234}, year = {2014}, language = {en} } @article{TyagiMalhotraThuenemannetal.2013, author = {Tyagi, Rahul and Malhotra, Shashwat and Th{\"u}nemann, Andreas F. and Sedighi, Amir and Weber, Marcus and Sch{\"a}fer, Andreas and Haag, Rainer}, title = {Investigations of Host-Guest Interactions with Shape-persistent Nonionic Dendritic Micelles}, volume = {117}, journal = {J. Phys. Chem. C}, number = {23}, pages = {12307 -- 12317}, year = {2013}, language = {de} } @article{ShanCarlsonBujotzeketal.2013, author = {Shan, Min and Carlson, Kathryn E. and Bujotzek, Alexander and Wellner, Anja and Gust, Ronald and Weber, Marcus and Katzenellenbogen, John A. and Haag, Rainer}, title = {Nonsteroidal Bivalent Estrogen Ligands - An Application of the Bivalent Concept to the Estrogen Receptor}, volume = {8}, journal = {ACS Chem. Biol.}, number = {4}, pages = {707 -- 715}, year = {2013}, language = {en} } @article{ShanBujotzekAbendrothetal.2011, author = {Shan, Min and Bujotzek, Alexander and Abendroth, Frank and Seitz, Oliver and Weber, Marcus and Haag, Rainer}, title = {Conformational Analysis of Bivalent Estrogen Receptor-Ligands: From Intramolecular to Intermolecular Binding}, journal = {ChemBioChem, 12(17)}, doi = {10.1002/cbic.201100529}, pages = {2587 -- 2598}, year = {2011}, language = {en} } @article{FrickeFrometaKerkhoffetal.2025, author = {Fricke, Mackenzie S. and Frometa, Magalee R. and Kerkhoff, Yannic and Bernhard, Samuel P. and Tahir, Ramat S. and Quaas, Elisa and Totten, William H. and Haag, Rainer and Achazi, Katharina and Cloninger, Mary J.}, title = {The toxicity, uptake, and impact on galectin-3 mediated apoptosis of lactose functionalized PAMAM dendrimers}, volume = {6}, journal = {Materials Advances}, doi = {10.1039/D4MA00782D}, pages = {3171 -- 3184}, year = {2025}, abstract = {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.}, language = {en} } @article{KhatriBobackAbdelwahabetal.2025, author = {Khatri, Vinod and Boback, Nico and Abdelwahab, Hassan and Niemeyer, Daniela and Palmer, Tahlia M. and Sahoo, Anil Kumar and Kerkhoff, Yannic and Ludwig, Kai and Balci, Dilara and Trimpert, Jakob and Haag, Rainer and Povolotsky, Tatyana L. and Netz, Roland R. and Drosten, Christian and Lauster, Daniel C. and Bhatia, Sumati}, title = {Polysialosides outperform sulfated analogs for the inhibition of SARS-CoV-2}, volume = {21}, journal = {Small}, number = {34}, doi = {10.1002/smll.202500719}, year = {2025}, abstract = {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.}, language = {en} } @article{LangHelfmeierStefanowskietal.2020, author = {Lang, Annemarie and Helfmeier, Sarah and Stefanowski, Jonathan and Kuppe, Aditi and Sunkara, Vikram and Pfeiffenberger, Moritz and Wolter, Angelique and Damerau, Alexandra and Hemmati-Sadeghi, Shabnam and Ringe, Jochen and Haag, Rainer and Hauser, Anja E. and L{\"o}hning, Max and Perka, Carsten and Duda, Georg and Hoff, Paula and Schmidt-Bleek, Katharina and Gaber, Timo and Buttgereit, Frank}, title = {HIF-stabilization prevents delayed fracture healing}, journal = {bioarxiv}, doi = {10.1101/2020.07.02.182832}, year = {2020}, language = {en} }