Researcher in the laboratory

Chemical Biology of Carbohydrates

Prof Dr Alexander Titz

Complex carbohydrates play a vital role in biological recognition processes that are represented by the presence of dense glycoconjugate layers on cells known as the glycocalyx. Despite their importance, the study of carbohydrates suffers from limited methods for their synthesis and analysis contrary to nucleic acids or proteins. The lab of Dr. Alexander Titz focuses on the development of novel glycomimetics to fight mechanisms of chronic bacterial infections such as biofilm formation of P. aeruginosa.

Our research and approach

Treatment of chronic infections: disrupting lectin-mediated biofilms

Many human pathogens can establish chronic infections with the help of a biofilm mode of life. As a protective shield, the matrix of the biofilm renders antibiotics ineffective and secures survival of the embedded pathogen. Novel ways for treatment address disintegration of such biofilms and thus restore activity of antibiotics. Frequently, the architecture of biofilms is maintained by carbohydrates and so-called lectins, recognizing and cross-linking carbohydrate motifs of the glycocalyx, both on human cells and pathogens. The inhibition of such structural components leads to the disruption of a biofilm and thereby allows treatment of the infection. Pseudomonas aeruginosa is an important pathogen in hospital-acquired infections and for cystic fibrosis patients. This Gram-negative bacterium can establish chronic infections in various tissues through assembly into protective biofilms. One focus of our research is two Pseudomonas aeruginosa lectins, which are crucial elements of the biofilm architecture.

The group of Dr. Alexander Titz aims at the development of antibacterial drugs using a combination of medicinal chemistry, biochemistry and microbiological methods. Recently, a competitive binding assay was developed for the in vitro evaluation of inhibitors of the Pseudomonas lectins. In collaboration with other groups at HIPS and the HZI, potent molecules obtained by the group are then further evaluated in biofilm and infection models. Such compounds may ultimately lead to successful treatment of chronic infections without evoking resistances among the pathogens.

Prof. Titz heads the Chair of Organic and Pharmaceutical Chemistry at Saarland University as well as the Chemical Biology of Carbohydrates group at the HZI/HIPS. The information about projects, staff, and publications on this website covers both groups.

Team members

Beshoy Tawfik

Beshoy Tawfik

PhD Student

Hanna Perius

Hanna Perius

PhD Student

Johanna Knigge

Johanna Knigge

PhD Student

Lisa Marie Denig

Lisa Marie Denig

PhD Student

Mario Fares

Mario Fares

PhD Student

Marta Czekanska

Marta Czekanska

PhD Student

Omar Zareei

Omar Zareei

PhD Student

Qiuyu Zhu

Qiuyu Zhu

PhD Student

Steffen Leusmann

Steffen Leusmann

PhD Student

Zeyue Zhang

Zeyue Zhang

PhD Student

Dirk Hauck

Dirk Hauck

Technical Assistant

Research projects

Sialomimetic Viral Entry Inhibitors - A route towards the first treatments for neglected human and emerging zoonotic viruses (Alexander Titz & Dominique Schols)

Zoonotic viruses can rapidly emerge from animals and transmit to humans as has been well documented for various avian/porcine influenza and bat corona viruses. It has now been observed repeatedly that these animal-to-human transmissions can result in a pandemic causing millions of deaths and a massive economic burden for humanity. All those pandemic viruses and numerous other classes of human viruses exploit animal and human sialic acid receptors for transmission and infection. Therefore, viral entry inhibitors interfering with this process are of broad interest. In this early discovery project, the development of novel sialomimetic therapeutics will be established. After initial validation using known viruses with known and distinct sialic acid binding specificity, the platform will then be applied onto viruses with reported but unexplored sialic acid binding, i.e. Parainfluenza, Zika and BK Polyoma Viruses, all of which currently lack drugs or vaccines. This pipeline will therefore yield sialomimetic entry inhibitors for the treatment of viral infections with clinical need, and importantly, the established workflow will serve as an important platform in the scope of Pandemic Preparedness.

Further information

Carbohydrate cOnjugates as Trojan horsE to improve Antibiotic iMport

The increase of antimicrobial resistance is a major threat for individual and public health. Consequently, new weapons to fight the emerging multidrug-resistant bacteria are quickly required. The ESKAPE pathogens are at the frontline of these problematic life-threatening drug resistant nosocomial pathogens. In this project, we aim to overcome antimicrobial resistance by hijacking energy-driven carbohydrate uptake systems (PTS and ABC transporters) to actively pump carbohydrate-antibiotic conjugates into bacteria which will be liberated by cellular glycosidases. These transporters are able to accumulate mM intracellular concentrations of their substrates. Exploring if they will boost intracellular concentrations of the carbohydrate-antibiotic conjugates as well is the main objective of the CO-TEAM project. Our preliminary work shows that the expression of the transporters of these carbohydrates is significantly induced under infection conditions. The project is divided into 4 tasks. 4 different oligosaccharide conjugates carrying 6 different antibiotics from 4 different classes will be chemically synthesized. These conjugates will then be studied for antimicrobial efficacy and resistance development against a panel of strains with a focus on the most urgent ESKAPE pathogens. In addition, mechanistic analyses to identify the transporters importing the conjugates will be conducted in 2 Gram-positive and 2 Gram-negative pathogens. Finally, we will evaluate the most promising conjugates in an insect and mouse model. Boosting intracellular antibiotic concentrations through active import is expected to overcome antimicrobial resistance mechanisms, both, target modifications lowering the antibiotic's efficacy, also permeability affecting resistance, the major problem in Gram-negative bacteria.

Futher Information


Bacterial infections are now a global threat demanding novel treatments due to the appearance of resistances against antibiotics at a high pace. The ESKAPE pathogens are those with highest importance in the EU and chronic infections due to biofilm formation are a particular task. Noninvasive pathogen-specific imaging of the infected tissue is not clinically available. Its successful implementation will enable the choice of appropriate therapy and boost efficacy. Furthermore,
Gram-negative bacteria have a highly protective cellular envelope as an important resistance mechanism for drugs acting intracellularly, resulting in an alarmingly empty drug-pipeline.
To overcome this gap, I will establish Lectin-directed Theranostics targeting pathogens via their extracellular carbohydrate-binding proteins at the site of infection for specific imaging and treatment. This will be implemented for the highly resistant ESKAPE pathogen Pseudomonas aeruginosa through 3 different work packages.
WP1 Sweet Imaging: Design & conjugation of lectin-directed ligands to imaging probes, Optimization of ligand/linker, in vivo proof-of-concept imaging study.
WP2 Sweet Targeting: Delivery of antibiotics to the infection through covalent linking of lectindirecting groups. Employing different antibiotics, assessment of bactericidal potency and targeting efficiency. Manufacturing of nano-carriers with surface exposed lectin-directed ligands, noncovalent charging with antibiotics. In vitro and in vivo targeting.
WP3 Sweet SMART Targeting: Conjugates as SMART drugs: specific release of anti-biofilm lectin inhibitor and drug cargo upon contact with pathogen, development of linkers cleavable by pathogenic enzymes.
SWEETBULLETS will establish fundamentally novel lectin-directed theranostics to fight these deleterious infections and provide relief to nosocomially infected and cystic fibrosis patients. It is rapidly extendable towards other ESKAPE pathogens, e.g. Klebsiella spp..

Further Information

Development of non-carbohydrate glycomimetics

Protein-carbohydrate interactions play a key role in the first step of numerous biological processes, e.g. fertilization and tissue homing of immune cells, but also in infection, inflammation, migration of tumor cells and other pathologies. Pathogenic microorganisms (viruses, bacteria, fungi and parasites) have developed strategies for utilizing glycan epitopes on human tissues for specific recognition, for adhesion and sometimes for cellular internalization. The proteins involved can be viral capsid domains, adhesins on top of pili, soluble lectins or carbohydrate binding domains of enzymes or toxins. Their carbohydrate-binding sites are specific for glycans located on human epithelia such as the histo/blood group oligosaccharides of ABO and Lewis systems. Molecules that could interfere with such lectin/glycan interaction are therefore of high interest as anti-infectious agents. Similarly human lectins are involved in chronic diseases related to inflammation and cancer, and consequently the search for lectin inhibitors to interfere with these pathological conditions is of outstanding interest. The project aims at the development of the underexplored area of non-carbohydrate drug-like lectin inhibitors. Such glycomimetics could overcome current limitations of carbohydrate-based therapeutics such as pharmacokinetic and pharmacodynamic limitations as well as synthetic tractability. Targeting three lectins from opportunistic bacteria, the consortium of two French and two German laboratories proposes to combine virtual and in vitro screening of chemical libraries using functional assays and NMR approaches, followed by structure (X-ray, NMR), thermodynamics (ITC) and kinetics (SPR, MD) guided lead optimization. Assembling of lead structures into oligomeric compounds in order to use natural lectin multivalency to gain very high affinity will be also envisaged. This project aims at the establishment of a broadly applicable methodology for the development of non-carbohydrate lectin inhibitors. A set of three diverse and representative bacterial lectins was chosen to explore the potential of the discovery pipeline. However, this approach will not be limited to bacterial targets and other viral, fungal, or human lectins of high therapeutic significance can be targeted as well. While pipeline development is our major concern, generating novel anti-infectives is foreseen (i.e. a problem-solving endeavor). Moreover, this endeavor will contribute to our fundamental understanding of biological processes involving multivalent receptors such as membrane dynamics and lipid raft-mediated internalization (i.e. a curiosity driven research).

Further Information



The resuscitation-promoting factor (Rpf) from Micrococcus luteus and its putative reaction product 1,6-anhydro-MurNAc increase culturability of environmental bacteria

Guzman J, Raval D, Hauck D, Titz A, Poehlein A, Degenkolb T, Daniel R, Vilcinskas A (2023)

Access microbiology 5 (9)DOI: 10.1099/acmi.0.000647.v4

Switch-on luminescent sensing of unlabelled bacterial lectin by terbium(III) glycoconjugate systems

Wojtczak K, Zahorska E, Murphy I, Koppel F, Cooke G, Titz A, Byrne J (2023)

Chem. Commun. (Cambridge, U. K.) 59 (54): 8384-8387DOI: 10.1039/D3CC02300A

Pseudomonas aeruginosa LecB suppresses immune responses by inhibiting transendothelial migration

Sponsel J, Guo Y, Hamzam L, Lavanant A, Pérez-Riverón A, Partiot E, Muller Q, Rottura J, Gaudin R, Hauck D, …, Römer W, Mueller C (2023)

EMBO reports 24 (4)DOI: 10.15252/embr.202255971

Tackling the outer membrane: facilitating compound entry into Gram-negative bacterial pathogens

Saxena D, Maitra R, Bormon R, Czekanska M, Meiers J, Titz A, Verma S, Chopra S (2023)

npj Antimicrob Resist 1 (1)DOI: 10.1038/s44259-023-00016-1

Glycomimetics for the inhibition and modulation of lectins

Leusmann S, Ménová P, Shanin E, Titz A, Rademacher C (2023)

Chem. Soc. Rev. 52 (11): 3663-3740DOI: 10.1039/d2cs00954d

Neutralizing the Impact of the Virulence Factor LecA from Pseudomonas aeruginosa on Human Cells with New Glycomimetic Inhibitors

Zahorska E, Rosato F, Stober K, Kuhaudomlarp S, Meiers J, Hauck D, Reith D, Gillon E, Rox K, Imberty A, Römer W, Titz A (2023)

Angewandte Chemie (International ed. in English) 62 (7)DOI: 10.1002/anie.202215535


Targeting undruggable carbohydrate recognition sites through focused fragment library design

Shanina E, Kuhaudomlarp S, Siebs E, Fuchsberger F, Denis M, da Silva Figueiredo Celestino Gomes P, Clausen M, Seeberger P, Rognan D, Titz A, Imberty A, Rademacher C (2022)

Commun Chem 5 (1): 1-11DOI: 10.1038/s42004-022-00679-3

NamZ1 and NamZ2 from the Oral Pathogen Tannerella forsythia Are Peptidoglycan Processing Exo-β-N-Acetylmuramidases with Distinct Substrate Specificities

Borisova M, Balbuchta K, Lovering A, Titz A, Mayer C (2022)

J. Bacteriol. 204 (3)DOI: 10.1128/jb.00597-21

Targeting the Central Pocket of the Pseudomonas aeruginosa Lectin LecA

Siebs E, Shanina E, Kuhaudomlarp S, da Silva Figueiredo Celestino Gomes P, Fortin C, Seeberger P, Rognan D, Rademacher C, Imberty A, Titz A (2022)

Chembiochem : a European journal of chemical biology 23 (3)DOI: 10.1002/cbic.202100563

β-Boronic Acid-Substituted Bodipy Dyes for Fluorescence Anisotropy Analysis of Carbohydrate Binding

Hoffmann C, Jourdain M, Grandjean A, Titz A, Jung G (2022)

Analytical chemistry 94 (16): 6112-6119DOI: 10.1021/acs.analchem.1c04654

Pineapple Lectin AcmJRL binds SARS-CoV-2 Spike Protein in a carbohydrate-dependent fashion

Meiers J, Dastbaz J, Adam S, Rasheed S, Kirsch S, Meiser P, Gross P, Müller R, Titz A (2022)

Chembiochem : a European journal of chemical biologyDOI: 10.1002/cbic.202200463

The Glycan-Specificity of the Pineapple Lectin AcmJRL and its Carbohydrate-Dependent Binding of the SARS-CoV-2 Spike Protein

Meiers J, Dastbaz J, Adam S, Rasheed S, Kirsch S, Meiser P, Gross P, Müller R, Titz A (2022)

BookDOI: 10.1101/2022.05.27.493400

Lectin-Targeted Prodrugs Activated by Pseudomonas aeruginosa for Self-Destructive Antibiotic Release

Meiers J, Rox K, Titz A (2022)

Journal of medicinal chemistry 65 (20): 13988-14014DOI: 10.1021/acs.jmedchem.2c01214

Discovery of N-β-l-Fucosyl Amides as High-Affinity Ligands for the Pseudomonas aeruginosa Lectin LecB

Mala P, Siebs E, Meiers J, Rox K, Varrot A, Imberty A, Titz A (2022)

Journal of medicinal chemistry 65 (20): 14180-14200DOI: 10.1021/acs.jmedchem.2c01373

Targeting extracellular lectins of Pseudomonas aeruginosa with glycomimetic liposomes

Metelkina O, Huck B, O'Connor J, Koch M, Manz A, Lehr C, Titz A (2022)

Journal of Materials Chemistry B 10 (4): 537-548DOI: 10.1039/d1tb02086b

Nano-in-Microparticles for Aerosol Delivery of Antibiotic-Loaded, Fucose-Derivatized, and Macrophage-Targeted Liposomes to Combat Mycobacterial Infections: In Vitro Deposition, Pulmonary Barrier Interactions, and Targeted Delivery

Huck B, Thiyagarajan D, Bali A, Boese A, Besecke K, Hozsa C, Gieseler R, Furch M, Carvalho-Wodarz C, Waldow F, …, Loretz B, Lehr C (2022)

Advanced healthcare materials 11 (11)DOI: 10.1002/adhm.202102117


Short Peptides and Their Mimetics as Potent Antibacterial Agents and Antibiotic Adjuvants

Panjla A, Kaul G, Chopra S, Titz A, Verma S (2021)

ACS chemical biology 16 (12): 2731-2745DOI: 10.1021/acschembio.1c00626

A Remote Secondary Binding Pocket Promotes Heteromultivalent Targeting of DC-SIGN

Wawrzinek R, Wamhoff E, Lefebre J, Rentzsch M, Bachem G, Domeniconi G, Schulze J, Fuchsberger F, Zhang H, Modenutti C, …, Ernst B, Rademacher C (2021)

J. Am. Chem. Soc. 143 (45): 18977-18988DOI: 10.1021/jacs.1c07235

Towards the sustainable discovery and development of new antibiotics

Miethke M, Pieroni M, Weber T, Brönstrup M, Hammann P, Halby L, Arimondo P, Glaser P, Aigle B, Bode H, …, Moser H, Müller R (2021)

Nature reviews. Chemistry 5 (10): 726-749DOI: 10.1038/s41570-021-00313-1

Non-Carbohydrate Glycomimetics as Inhibitors of Calcium(II)-Binding Lectins

Kuhaudomlarp S, Siebs E, Shanina E, Topin J, Joachim I, da Silva Figueiredo Celestino Gomes P, Varrot A, Rognan D, Rademacher C, Imberty A, Titz A (2021)

Angew. Chem. Int. Ed. 60 (15): 8104-8114DOI: 10.1002/anie.202013217

The exo-β-N-acetylmuramidase NamZ from Bacillus subtilis is the founding member of a family of exo-lytic peptidoglycan hexosaminidases

Müller M, Calvert M, Hottmann I, Kluj R, Teufel T, Balbuchta K, Engelbrecht A, Selim K, Xu Q, Borisova M, Titz A, Mayer C (2021)

The Journal of biological chemistry 296DOI: 10.1016/j.jbc.2021.100519


Protein-observed 19F NMR of LecA from Pseudomonas aeruginosa

Shanina E, Siebs E, Zhang H, Silva D, Joachim I, Titz A, Rademacher C (2020)

GlycobiologyDOI: 10.1093/glycob/cwaa057

Directing Drugs to Bugs: Antibiotic-Carbohydrate Conjugates Targeting Biofilm-Associated Lectins of Pseudomonas aeruginosa

Meiers J, Zahorska E, Röhrig T, Hauck D, Wagner S, Titz A (2020)

Journal of medicinal chemistry 63 (20): 11707-11724DOI: 10.1021/acs.jmedchem.0c00856

A rapid synthesis of low-nanomolar divalent LecA inhibitors in four linear steps from d -galactose pentaacetate

Zahorska E, Kuhaudomlarp S, Minervini S, Yousaf S, Lepsik M, Kinsinger T, Hirsch A, Imberty A, Titz A (2020)

Chem. Commun. 56 (62): 8822-8825DOI: 10.1039/d0cc03490h

Expression, Purification, and Functional Characterization of Tectonin 2 from Laccaria bicolor: A Six-Bladed Beta-Propeller Lectin Specific for O-Methylated Glycans

Wohlschlager T, Titz A, Künzler M, Varrot A (2020)

Methods Mol Biol 2132: 669-682DOI: 10.1007/978-1-0716-0430-4_58


Lectin antagonists in infection, immunity, and inflammation

Meiers J, Siebs E, Zahorska E, Titz A (2019)

Current opinion in chemical biology 53: 51-67DOI: 10.1016/j.cbpa.2019.07.005

Anti-biofilm Agents against Pseudomonas aeruginosa: A Structure-Activity Relationship Study of C-Glycosidic LecB Inhibitors

Sommer R, Rox K, Wagner S, Hauck D, Henrikus S, Newsad S, Arnold T, Ryckmans T, Brönstrup M, Imberty A, …, Hartmann R, Titz A (2019)

Journal of medicinal chemistry 62 (20): 9201-9216DOI: 10.1021/acs.jmedchem.9b01120

Chemical synthesis of tripeptide thioesters for the biotechnological incorporation into the myxobacterial secondary metabolite argyrin via mutasynthesis

Siebert D, Sommer R, Pogorevc D, Hoffmann M, Wenzel S, Müller R, Titz A (2019)

Beilstein journal of organic chemistry 15: 2922-2929DOI: 10.3762/bjoc.15.286

Induction of rare conformation of oligosaccharide by binding to calcium-dependent bacterial lectin: X-ray crystallography and modelling study

Lepsik M, Sommer R, Kuhaudomlarp S, Lelimousin M, Paci E, Varrot A, Titz A, Imberty A (2019)

European journal of medicinal chemistry 177: 212-220DOI: 10.1016/j.ejmech.2019.05.049


Bivalent LecA inhibitors targeting Pseudomonas aeruginosa LecA

Zahorska E, Minervini S, Kuhaudomlarp S, Imberty A, Titz A (2018)

Patent (EP19306432.6)

N-Acetylmuramic Acid (MurNAc) Auxotrophy of the Oral Pathogen Tannerella forsythia: Characterization of a MurNAc Kinase and Analysis of Its Role in Cell Wall Metabolism

Hottmann I, Mayer V, Tomek M, Friedrich V, Calvert M, Titz A, Schäffer C, Mayer C (2018)

Frontiers in microbiology 9DOI: 10.3389/fmicb.2018.00019

Crystal Structures of Fungal Tectonin in Complex with O-Methylated Glycans Suggest Key Role in Innate Immune Defense

Sommer R, Makshakova O, Wohlschlager T, Hutin S, Marsh M, Titz A, Künzler M, Varrot A (2018)

Structure (London, England : 1993) 26 (3): 391-402DOI: 10.1016/j.str.2018.01.003

Glycomimetic, Orally Bioavailable LecB Inhibitors Block Biofilm Formation of Pseudomonas aeruginosa

Sommer R, Wagner S, Rox K, Varrot A, Hauck D, Wamhoff E, Schreiber J, Ryckmans T, Brunner T, Rademacher C, …, Imberty A, Titz A (2018)

Journal of the American Chemical Society 140 (7): 2537-2545DOI: 10.1021/jacs.7b11133

Virtual Screening Against Carbohydrate-Binding Proteins: Evaluation and Application to Bacterial Burkholderia ambifaria Lectin

Dingjan T, Gillon É, Imberty A, Pérez S, Titz A, Ramsland P, Yuriev E (2018)

Journal of chemical information and modeling 58 (9): 1976-1989DOI: 10.1021/acs.jcim.8b00185

Pathoblockers or antivirulence drugs as a new option for the treatment of bacterial infections

Calvert M, Jumde V, Titz A (2018)

Beilstein journal of organic chemistry 14: 2607-2617DOI: 10.3762/bjoc.14.239


An efficient synthesis of 1,6-anhydro-N-acetylmuramic acid from N-acetylglucosamine

Calvert M, Mayer C, Titz A (2017)

Beilstein journal of organic chemistry 13: 2631-2636DOI: 10.3762/bjoc.13.261

Covalent Lectin Inhibition and Application in Bacterial Biofilm Imaging

Wagner S, Hauck D, Hoffmann M, Sommer R, Joachim I, Müller R, Imberty A, Varrot A, Titz A (2017)

Angewandte Chemie (International ed. in English) 56 (52): 16559-16564DOI: 10.1002/anie.201709368

Photorhabdus luminescens lectin A (PllA): A new probe for detecting α-galactoside-terminating glycoconjugates

Beshr G, Sikandar A, Jemiller E, Klymiuk N, Hauck D, Wagner S, Wolf E, Koehnke J, Titz A (2017)

J Biol Chem 292 (48): 19935-19951DOI: 10.1074/jbc.M117.812792

Ciprofloxacin-loaded lipid-core nanocapsules as mucus penetrating drug delivery system intended for the treatment of bacterial infections in cystic fibrosis

Torge A, Wagner S, Chaves P, Oliveira E, Guterres S, Pohlmann A, Titz A, Schneider M, Beck R (2017)

Int J Pharm 527 (1-2): 92-102DOI: 10.1016/j.ijpharm.2017.05.013

Efficient Two Step β-Glycoside Synthesis from N-Acetyl d-Glucosamine: Scope and Limitations of Copper(II) Triflate-Catalyzed Glycosylation

Sommer R, Hauck D, Titz A (2017)

ChemistrySelect 2 (15)DOI: 10.1002/slct.201700161

Photoswitchable Janus glycodendrimer micelles as multivalent inhibitors of LecA and LecB from Pseudomonas aeruginosa

Hu Y, Beshr G, Garvey C, Tabor R, Titz A, Wilkinson B (2017)

Colloids and surfaces. B, Biointerfaces 159: 605-612DOI: 10.1016/j.colsurfb.2017.08.016


Novel Strategies for the Treatment of Pseudomonas aeruginosa Infections

Wagner S, Sommer R, Hinsberger S, Lu C, Hartmann R, Empting M, Titz A (2016)

Journal of medicinal chemistry 59 (13): 5929-69DOI: 10.1021/acs.jmedchem.5b01698

Inhibitors of Pseudomonas aeruginosa LecB

Sommer R, Titz A (2016)

Patent (WO2016/151066 A1)

O-Alkylated heavy atom carbohydrate probes for protein X-ray crystallography: Studies towards the synthesis of methyl 2-O-methyl-L-selenofucopyranoside

Sommer R, Hauck D, Varrot A, Imberty A, Künzler M, Titz A (2016)

Beilstein journal of organic chemistry 12: 2828-2833DOI: 10.3762/bjoc.12.282

Development of a competitive binding assay for the Burkholderia cenocepacia lectin BC2L-A and structure activity relationship of natural and synthetic inhibitors

Beshr G, Sommer R, Hauck D, Siebert D, Hofmann A, Imberty A, Titz A (2016)

Med Chem Commun 7 (3): 519-530DOI: 10.1039/C5MD00557D

Development and optimization of a competitive binding assay for the galactophilic low affinity lectin LecA from Pseudomonas aeruginosa

Joachim I, Rikker S, Hauck D, Ponader D, Boden S, Sommer R, Hartmann L, Titz A (2016)

Org. Biomol. Chem. 14 (33): 7933-48DOI: 10.1039/c6ob01313a

The virulence factor LecB varies in clinical isolates: consequences for ligand binding and drug discovery

Sommer R, Wagner S, Varrot A, Nycholat C, Khaledi A, Häussler S, Paulson J, Imberty A, Titz A (2016)

Chem Sci 7 (8): 4990-5001DOI: 10.1039/c6sc00696e


Bisecting Galactose as a Feature of N-Glycans of Wild-type and Mutant Caenorhabditis elegans

Yan S, Brecker L, Jin C, Titz A, Dragosits M, Karlsson N, Jantsch V, Wilson I, Paschinger K (2015)

Mol Cell Proteomics 14 (8): 2111-25DOI: 10.1074/mcp.M115.049817

Cinnamide Derivatives of d-Mannose as Inhibitors of the Bacterial Virulence Factor LecB from Pseudomonas aeruginosa

Sommer R, Hauck D, Varrot A, Wagner S, Audfray A, Prestel A, Möller H, Imberty A, Titz A (2015)

ChemistryOpen 4 (6): 756-67DOI: 10.1002/open.201500162

Parasite Glycobiology: A Bittersweet Symphony

Rodrigues J, Acosta-Serrano A, Aebi M, Ferguson M, Routier F, Schiller I, Soares S, Spencer D, Titz A, Wilson I, Izquierdo L (2015)

PLoS Pathog. 11 (11)DOI: 10.1371/journal.ppat.1005169

Synthesis of mannoheptose derivatives and their evaluation as inhibitors of the lectin LecB from the opportunistic pathogen Pseudomonas aeruginosa

Hofmann A, Sommer R, Hauck D, Stifel J, Göttker-Schnetmann I, Titz A (2015)

Carbohydrate research 412: 34-42DOI: 10.1016/j.carres.2015.04.010


Methylated glycans as conserved targets of animal and fungal innate defense

Wohlschlager T, Butschi A, Grassi P, Sutov G, Gauss R, Hauck D, Schmieder S, Knobel M, Titz A, Dell A, …, Aebi M, Künzler M (2014)

Proceedings of the National Academy of Sciences of the United States of America 111 (27): 2787-96DOI: 10.1073/pnas.1401176111

A biophysical study with carbohydrate derivatives explains the molecular basis of monosaccharide selectivity of the Pseudomonas aeruginosa lectin LecB

Sommer R, Exner T, Titz A (2014)

PLoS ONE 9 (11)DOI: 10.1371/journal.pone.0112822

Amphiphilic cationic β(3R3)-peptides: membrane active peptidomimetics and their potential as antimicrobial agents

Mosca S, Keller J, Azzouz N, Wagner S, Titz A, Seeberger P, Brezesinski G, Hartmann L (2014)

Biomacromolecules 15 (5): 1687-95DOI: 10.1021/bm500101w


Glycomimetics as Pseudomonas aeruginosa lectin inhibitors

Titz A (2013)

Patent (WO2013152848A1)

New approaches to control infections: anti-biofilm strategies against gram-negative bacteria

Sommer R, Joachim I, Wagner S, Titz A (2013)

Chimia (Aarau) 67 (4): 286-90DOI: 10.2533/chimia.2013.286

Biofilme Neue Forschungsansätze zur Therapie bakterieller Infektionskrankheiten

Titz A (2013)

GIT Labor-Fachzeitschrift (2): 120-121

Discovery of two classes of potent glycomimetic inhibitors of Pseudomonas aeruginosa LecB with distinct binding modes

Hauck D, Joachim I, Frommeyer B, Varrot A, Philipp B, Möller H, Imberty A, Exner T, Titz A (2013)

ACS chemical biology 8 (8): 1775-84DOI: 10.1021/cb400371r


Conformational Constraints: Nature Does It Best with Sialyl Lewis x

Titz A, Marra A, Cutting B, Smieško M, Papandreou G, Dondoni A, Ernst B (2012)

Eur. J. Org. Chem. 2012 (28)DOI: 10.1002/ejoc.201200744


Core beta-galactosyltransferase and uses thereof

Titz A, Butschi A, Aebi M, Wilson I, Hengartner M, Künzler M (2010)

Patent (WO2010/136209A1)

Caenorhabditis elegans N-glycan core beta-galactoside confers sensitivity towards nematotoxic fungal galectin CGL2

Butschi A, Titz A, Wälti M, Olieric V, Paschinger K, Nöbauer K, Guo X, Seeberger P, Wilson I, Aebi M, Hengartner M, Künzler M (2010)

PLoS Pathog. 6 (1)DOI: 10.1371/journal.ppat.1000717

Probing the carbohydrate recognition domain of E-selectin: the importance of the acid orientation in sLex mimetics

Titz A, Patton J, Smiesko M, Radic Z, Schwardt O, Magnani J, Ernst B (2010)

Bioorg Med Chem 18 (1): 19-27DOI: 10.1016/j.bmc.2009.11.024


Molecular basis for galactosylation of core fucose residues in invertebrates: identification of caenorhabditis elegans N-glycan core alpha1,6-fucoside beta1,4-galactosyltransferase GALT-1 as a member of a novel glycosyltransferase family

Titz A, Butschi A, Henrissat B, Fan Y, Hennet T, Razzazi-Fazeli E, Hengartner M, Wilson I, Künzler M, Aebi M (2009)

J Biol Chem 284 (52): 36223-33DOI: 10.1074/jbc.M109.058354


Is adamantane a suitable substituent to pre-organize the acid orientation in E-selectin antagonists?

Titz A, Patton J, Alker A, Porro M, Schwardt O, Hennig M, Francotte E, Magnani J, Ernst B (2008)

Bioorg Med Chem 16 (2): 1046-56DOI: 10.1016/j.bmc.2007.07.025


Mimetics of Sialyl Lewis<sup>x</sup>: The Pre-Organization of the Carboxylic Acid is Essential for Binding to Selectins

Titz A, Ernst B (2007)

CHIMIA 61 (4): 194-197DOI: 10.2533/chimia.2007.194


A safe and convenient method for the preparation of triflyl azide, and its use in diazo transfer reactions to primary amines

Titz A, Radic Z, Schwardt O, Ernst B (2006)

Tetrahedron Lett. 47 (14)DOI: 10.1016/j.tetlet.2006.01.157

Complexation of copper(II)-Chelidamate: A multifrequency-pulsed electron paramagnetic resonance and electron nuclear double resonance analysis

Ramic E, Eichel R, Dinse K, Titz A, Schmidt B (2006)

J. Phys. Chem. B 110 (41): 20655-63DOI: 10.1021/jp061940u


Electrochemical synthesis of dimerizing and nondimerizing orthoquinone monoketals

Deffieux D, Fabre I, Titz A, Léger J, Quideau S (2004)

The Journal of organic chemistry 69 (25): 8731-8DOI: 10.1021/jo048677i

Copper dipicolinates as peptidomimetic ligands for the Src SH2 domain

Schmidt B, Jiricek J, Titz A, Ye G, Parang K (2004)

Bioorg Med Chem Lett 14 (16): 4203-6DOI: 10.1016/j.bmcl.2004.06.018