Orthogonal photoswitching of heterobivalent azobenzene glycoclusters: the effect of glycoligand orientation in bacterial adhesion

• Leon M. Friedrich and
• Thisbe K. Lindhorst

Beilstein J. Org. Chem. 2025, 21, 736–748, doi:10.3762/bjoc.21.57

• - and heteromultivalency effects are crucial [8][9][10][11][12], but also many other aspects of glycoligand presentation govern carbohydrate recognition. Interestingly, even a subtle structural variation in heterobivalent glycoclusters can result in unexpected differences in lectin binding due to

Photoswitchable glycoligands targeting Pseudomonas aeruginosa LecA

• Yu Fan,
• Ahmed El Rhaz,
• Stéphane Maisonneuve,
• Emilie Gillon,
• Maha Fatthalla,
• Franck Le Bideau,
• Guillaume Laurent,
• Samir Messaoudi,
• Anne Imberty and
• Juan Xie

Beilstein J. Org. Chem. 2024, 20, 1486–1496, doi:10.3762/bjoc.20.132

• is introduced on the azobenzene to increase the water solubility. The influence of ortho, meta, and para-substitution patterns of the azobenzene on the lectin binding has also been studied. Synthesis The β-O-galactosyl p,p'-bis-substituted azobenzene derivative 1 was prepared from galactose and

Elucidating the glycan-binding specificity and structure of Cucumis melo agglutinin, a new R-type lectin

• Jon Lundstrøm,
• Emilie Gillon,
• Valérie Chazalet,
• Nicole Kerekes,
• Antonio Di Maio,
• Ten Feizi,
• Yan Liu,
• Annabelle Varrot and
• Daniel Bojar

Beilstein J. Org. Chem. 2024, 20, 306–320, doi:10.3762/bjoc.20.31

• answer the question whether CMA1 was a functional lectin and, if yes, what its binding specificity was. The standard approach to elucidate lectin binding specificity is via glycan array experiments. Here, tagged soluble lectin is added to, often, immobilized glycans and bound lectin is quantified via

Synthesis of the 3’-O-sulfated TF antigen with a TEG-N₃ linker for glycodendrimersomes preparation to study lectin binding

• Mark Reihill,
• Hanyue Ma,
• Dennis Bengtsson and
• Stefan Oscarson

Beilstein J. Org. Chem. 2024, 20, 173–180, doi:10.3762/bjoc.20.17

GlycoBioinformatics

• Kiyoko F. Aoki-Kinoshita,
• Frédérique Lisacek,
• Niclas Karlsson,
• Daniel Kolarich and
• Nicolle H. Packer

Beilstein J. Org. Chem. 2021, 17, 2726–2728, doi:10.3762/bjoc.17.184

• paper by Mehta et al. [5], who summarize recent developments and available online resources for glycan array data, a very powerful technique for understanding the structural element(s) of glycans required for different lectin binding. This further emphasizes the role of glycans as mediators of cellular

Targeted photoswitchable imaging of intracellular glutathione by a photochromic glycosheet sensor

• Xianzhi Chai,
• Hai-Hao Han,
• Yi Zang,
• Jia Li,
• Xiao-Peng He,
• Junji Zhang and
• He Tian

Beilstein J. Org. Chem. 2019, 15, 2380–2389, doi:10.3762/bjoc.15.230

• cell lines, endowing our hybrid sensor with specific cell target ability [35]. The cytoselectivity of the Glyco-DTE reporter was firstly checked in PBS buffer through lectin binding experiments. The lectin used here, peanut agglutinin (PNA), can selectively bind with β-ᴅ-galactoside that mimics the

Towards the preparation of synthetic outer membrane vesicle models with micromolar affinity to wheat germ agglutinin using a dialkyl thioglycoside

• Dimitri Fayolle,
• Nathalie Berthet,
• Bastien Doumeche,
• Olivier Renaudet,
• Peter Strazewski and
• Michele Fiore

Beilstein J. Org. Chem. 2019, 15, 937–946, doi:10.3762/bjoc.15.90

• 8 showed the highest inhibitory effect of this study with an IC50 of 11 µM corresponding to a 3000-fold improvement compared to the monomer control. This result suggests a higher participation of sugar units in the lectin binding for this compound. Docking calculation for model glycolipids To

What contributes to an effective mannose recognition domain?

• Christoph P. Sager,
• Deniz Eriş,
• Martin Smieško,
• Rachel Hevey and
• Beat Ernst

Beilstein J. Org. Chem. 2017, 13, 2584–2595, doi:10.3762/bjoc.13.255

• desolvation are often neglected. Because of the large number of hydroxy groups present in carbohydrate ligands, and the polar amino acid side chains of the lectin binding sites, desolvation generates an essential enthalpic penalty which can hardly be compensated for by the newly formed electrostatic

Orthogonal dual-modification of proteins for the engineering of multivalent protein scaffolds

• Michaela Mühlberg,
• Michael G. Hoesl,
• Christian Kuehne,
• Jens Dernedde,
• Nediljko Budisa and
• Christian P. R. Hackenberger

Beilstein J. Org. Chem. 2015, 11, 784–791, doi:10.3762/bjoc.11.88

• oxidative aldehyde formation at the N-terminus with NaIO4 [36][37][38][39][40][41]. With this approach, we aimed to engineer an artificial lectin-binding protein via chemical installation of several galactose moieties by CuAAC [18]. The second functionalization site at the protein’s N-terminus was

• lectin binding studies To ensure the stability of TTL throughout the dual-labeling process, we performed a lipase activity assay to demonstrate that the enzymatic activity could be retained. All protein samples thereby showed similar lipase activity, as determined by the colorimetric p-nitrophenol assay

• (see Supporting Information File 1). Finally, we also conducted surface plasmon resonance (SPR) studies to show the general applicability of our dual modified protein scaffold for measuring lectin binding constants (Figure 2 and Supporting Information File 1). We first probed the qualitative binding of

Probing multivalency in ligand–receptor-mediated adhesion of soft, biomimetic interfaces

• Stephan Schmidt,
• Hanqing Wang,
• Daniel Pussak,
• Simone Mosca and
• Laura Hartmann

Beilstein J. Org. Chem. 2015, 11, 720–729, doi:10.3762/bjoc.11.82

• water and drying. ConA (0.2 mg mL−1) in PBS buffer pH 7.4 was placed on the aldehyde-functionalized surfaces for 1 h [19]. and prior to the measurements washed with lectin binding buffer (10 mM HEPES pH 6, 50 mM NaCl, 1 mM MnCl2, 1 mM CaCl2). Reflection interference contrast microscopy (RICM) RICM on an

• domain NIH) and the mathematical software OriginPro (OriginLab, USA). 1 mL of lectin binding buffer pH 6 was added to the ConA-functionalized surface and PEG-Man SCPs were spread into the solution. The particles were sedimented and the contact radius and the particle radius were measured. Inhibition of

• the interaction was done by adding of α-methyl-D-mannose (300 µL, 1 mg mL−1) in lectin binding buffer to the suspension and well mixed so that all bound particles were detached from the surface. SCP adhesion measurement sketch (top): A mannose-functionalized PEG-SCP sediments onto a Concanavalin A

Convergent synthetic methodology for the construction of self-adjuvanting lipopeptide vaccines using a novel carbohydrate scaffold

• Vincent Fagan,
• Istvan Toth and
• Pavla Simerska

Beilstein J. Org. Chem. 2014, 10, 1741–1748, doi:10.3762/bjoc.10.181

• gave the novel carbohydrate building block 1 in 31% overall yield (Scheme 2). Similar carbohydrates have been used for the preparation of glycoclusters for lectin binding [25][26][27][28] and as scaffold carriers of multiple peptide antigens [17][29]. However, the synthesis of the new carbohydrate

Clicked and long spaced galactosyl- and lactosylcalix[4]arenes: new multivalent galectin-3 ligands

• Silvia Bernardi,
• Paola Fezzardi,
• Gabriele Rispoli,
• Stefania E. Sestito,
• Francesco Peri,
• Francesco Sansone and
• Alessandro Casnati

Beilstein J. Org. Chem. 2014, 10, 1672–1680, doi:10.3762/bjoc.10.175

• . Furthermore, we confirmed that in case of this specific lectin binding the presentation of lactose units on a cone calixarene is highly preferred with respect to its isomeric form in the 1,3-alternate structure. Keywords: glycocalixarenes; cluster glycoside effect; multivalency; click chemistry; surface

Photoswitchable precision glycooligomers and their lectin binding

• Daniela Ponader,
• Sinaida Igde,
• Marko Wehle,
• Katharina Märker,
• Mark Santer,
• David Bléger and
• Laura Hartmann

Beilstein J. Org. Chem. 2014, 10, 1603–1612, doi:10.3762/bjoc.10.166

• azobenzene unit allows for the photosensitive control of glycoligand binding to protein receptors. These stimuli-sensitive glycoligands promote the understanding of multivalent binding and will be further developed as novel biosensors. Keywords: azobenzene; glycopolymer; lectin binding; multivalency

• )-5 Z-isomers is anticipated to be very similar since their two azo units were found to operate independently. The long-lived Z-forms of these glycoconjugates allows for a convenient handling of the PSS mixtures and a precise measurement of their binding affinities. Lectin binding studies Competition

• affinity towards PA-IL lectins on demand, we were intrigued in the ability of our light-responsive systems to work when immobilized on a surface. To this end we attached the photoswitchable precision glycooligomers directly to the SPR chip and performed a second set of lectin binding experiments using SPR

Molecular architecture with carbohydrate functionalized β-peptides adopting 3₁₄-helical conformation

• Nitin J. Pawar,
• Navdeep S. Sidhu,
• George M. Sheldrick,
• Dilip D. Dhavale and
• Ulf Diederichsen

Beilstein J. Org. Chem. 2014, 10, 948–955, doi:10.3762/bjoc.10.93

• , xylose) as sugar-β-amino acids in a 314-helix. Up to three sugar units were linearly aligned with 5 Å distance (Figure 1). This kind of sugar organization will be of later relevance, e.g., in lectin binding studies and with respect to the investigation of multivalency effects [21][22][23]. The use of

Mannose-decorated cyclodextrin vesicles: The interplay of multivalency and surface density in lectin–carbohydrate recognition

• Ulrike Kauscher and
• Bart Jan Ravoo

Beilstein J. Org. Chem. 2012, 8, 1543–1551, doi:10.3762/bjoc.8.175

• to multivalent interaction at the vesicle surface. In addition, we increased the number of mannose units in the guest molecule, assuming that a high density of carbohydrate is essential for multivalent lectin binding at the vesicle surface. Results and Discussion Four different guest molecules were

Synthetic glycopeptides and glycoproteins with applications in biological research

• Ulrika Westerlind

Beilstein J. Org. Chem. 2012, 8, 804–818, doi:10.3762/bjoc.8.90

• and lectin binding [95][96][97][98][99][100][101][102][103][104][105]. The synthesis of glycoclusters/dendrimers is an area of research aimed at tackling the increasing problems with bacterial multi-antibiotic resistance. Microbe adherence to the glycans on the tissue cell surface is essential for an

• microbe and lectin binding studies, glycopeptide based glycoclusters/dendrimers were applied, employing linear peptide backbones, cyclic peptide scaffolds or multi-lysine scaffolds [106][107][108][109][110][111][112][113][114][115][116][117][118]. The pentavalent cholera toxin protein secreted by Vibrio

Formation of carbohydrate-functionalised polystyrene and glass slides and their analysis by MALDI-TOF MS

• Martin J. Weissenborn,
• Johannes W. Wehner,
• Christopher J. Gray,
• Robert Šardzík,
• Claire E. Eyers,
• Thisbe K. Lindhorst and
• Sabine L. Flitsch

Beilstein J. Org. Chem. 2012, 8, 753–762, doi:10.3762/bjoc.8.86

• generally confirmed indirectly by lectin binding, which severely limits the ligands that can be interrogated to those that can be detected by carbohydrate-binding proteins. To overcome this limitation, we were interested in developing label-free methods for ligand detection on these polystyrene surfaces

Chemo-enzymatic modification of poly-N-acetyllactosamine (LacNAc) oligomers and N,N-diacetyllactosamine (LacDiNAc) based on galactose oxidase treatment

• Christiane E. Kupper,
• Ruben R. Rosencrantz,
• Birgit Henßen,
• Helena Pelantová,
• Stephan Thönes,
• Anna Drozdová,
• Vladimir Křen and
• Lothar Elling

Beilstein J. Org. Chem. 2012, 8, 712–725, doi:10.3762/bjoc.8.80

• -containing glycans trigger the cellular immune response of natural killer cells [10][11][12]. Scientific interest in the synthesis of naturally occurring and modified LacNAc and poly-LacNAc glycans is high, as they can be used for the detailed investigation of lectin binding modes and their biological