Interaction Of Lectin Research Articles

Lectin Analysis of SARS-CoV-2-Positive Nasopharyngeal Samples Using GLYcoPROFILE® Technology Platform.

Nasopharyngeal samples are currently accepted as the standard diagnostic samples for nucleic acid amplification testing and antigenic testing for the SARS-CoV-2 virus. In addition to the diagnostic capacity of SARS-CoV-2-positive crude nasopharyngeal samples, their qualitative potential for direct glycan-specific analysis, in order to uncover unique glycol profiles, was assessed. In this study we provide glycan characterization of SARS-CoV-2-positive and -negative nasopharyngeal samples directly from lectin interactions. Although with limited throughput, this study evaluated the clinical sensitivity and specificity of the GLYcoPROFILE® technology platformon45crude nasopharyngeal samples collected between November 2020 and April 2022. Each GLYcoPROFILE® of 39 SARS-CoV-2-positive samples was compared toglycoprofiling on a panel of 10 selected lectins and the results were paralleled with SARS-CoV-2-negative samples' results. The GLYcoPROFILE® showed a clear distinction between positive and negative samples with WFA, GSL-II, PHA-L (GlcNAc-specific) and BPA (GalNAc-specific) highlighted as relevant lectins in SARS-CoV-2-positive samples. In addition, a significant, positive statistical correlation was found for these lectins (p < 0.01).

The staphylococcal biofilm protein Aap mediates cell-cell adhesion through mechanically distinct homophilic and lectin interactions.

The accumulation phase of staphylococcal biofilms relies on both the production of an extracellular polysaccharide matrix and the expression of bacterial surface proteins. A prototypical example of such adhesive proteins is the long multidomain protein Aap (accumulation-associated protein) from Staphylococcus epidermidis, which mediates zinc-dependent homophilic interactions between Aap B-repeat regions through molecular forces that have not been investigated yet. Here, we unravel the remarkable mechanical strength of single Aap-Aap homophilic bonds between living bacteria and we demonstrate that intercellular adhesion also involves sugar binding through the lectin domain of the Aap A region. We find that the mechanical force needed to unfold individual β-sheet-rich G5-E domains from the Aap B-repeat regions is very high, ranging from 300 up to 1,000 pN at high loading rates, indicating these are extremely stable. This high mechanostability provides a means to the cells to form highly adhesive and cohesive biofilms capable of sustaining high physiological shear stress. Importantly, we identify a previously undescribed role of Aap in bacterial-bacterial adhesion, that is, heterophilic sugar binding by a specific lectin domain located in the N-terminal A region, which might be important to establish initial contacts between cells before strong homophilic bonds come into play. This study emphasizes the remarkable mechanical and binding properties of Aap as well as its wide diversity of adhesive functions.

Lectin Histochemistry: Historical Perspectives, State of the Art, and Future Directions.

Lectins, discovered more than 100years ago and defined by their ability to selectively recognize specific carbohydrate structures, are ubiquitous in living organisms. Their precise functions are as yet under-explored and incompletely understood but they are clearly involved, through recognition of their binding partners, in a myriad of biological mechanisms involved in cell identity, adhesion, signaling, and growth regulation in health and disease. Understanding the complex "sugar code" represented by the "glycome" is a major challenge and at the forefront of current biological research. Lectins have been widely employed in histochemical studies to map glycosylation in cells and tissues. Here, a brief history of the discovery of lectins and early developments in their use is presented along with a selection of some of the most interesting and significant discoveries to emerge from theuse of lectin histochemistry. Further, an evaluation of the next generation of lectin-based technologies is presented, including the potential for designing recombinant lectins with more precisely defined binding characteristics, linking lectin-based studies with other technologies to answer fundamental questions in glycobiology and approaches to exploring the interactions of lectins with their binding partners in more detail.

Lectins from plants and algae act as anti-viral against HIV, influenza and coronaviruses.

BackgroundCarbohydrate–lectin interactions are extremely specific as the lectin is capable of recognising monomeric and oligomeric sugars in a reversible manner. It has been known for a long time that lectins have antibacterial, antifungal, and insecticidal activities. Recently, it has been reported that many lectins can prevent the virus growth by interacting with the viral envelop surface glycoprotein. Spike protein, which is found on the surface of some enveloped viruses, is heavily mannosylated and will have strong affinity for mannose specific lectins. According to the findings, lectins have a high binding affinity for the glycans of the SARS-CoV-2 spike glycoprotein, which contains N-glycosylation sites. As a result, various lectins are being researched and developed as anti-viral agents.ResultsAccording to our in silico studies, the amino acid residues Asn487, Tyr489, Gln493, Lys417, and Tyr505 of the receptor binding domain (RBD) of SARS-CoV-2 formed an interaction with the model lectin Lablab purpureus lectin. Similar interaction for SARS-CoV-2 spike protein was observed with Griffithsin lectin (algal source) as well. These observations demonstrate that lectins could be one of the potential molecules for neutralising coronavirus infection.ConclusionThis review focuses on anti-viral lectins isolated and characterized from plants and algae (last 5 years) and showed anti-viral properties against HIV, Influenza, and coronaviruses.

Seminal Plasma Glycoproteins as Potential Ligands of Lectins Engaged in Immunity Regulation.

Environmental pollution, chronic stress, and unhealthy lifestyle are factors that negatively affect reproductive potential. Currently, 15–20% of couples in industrialized countries face the problem of infertility. This growing health and social problem prompts researchers to explore the regulatory mechanisms that may be important for successful fertilization. In recent years, more attention has been paid to male infertility factors, including the impact of seminal plasma components on regulation of the female immune response to allogenic sperm, embryo and fetal antigens. Directing this response to the tolerogenic pathway is crucial to achieve a healthy pregnancy. According to the fetoembryonic defense hypothesis, the regulatory mechanism may be associated with the interaction of lectins and immunomodulatory glycoepitopes. Such interactions may involve lectins of dendritic cells and macrophages, recruited to the cervical region immediately after intercourse. Carbohydrate binding receptors include C type lectins, such as DC-SIGN and MGL, as well as galectins and siglecs among others. In this article we discuss the expression of the possible lectin ligands, highly fucosylated and high mannose structures, which may be recognized by DC-SIGN, glycans of varying degrees of sialylation, which may differ in their interaction with siglecs, as well as T and Tn antigens in O-glycans.

Systematic Optimisation of Microtiter Plate Lectin Assay to Improve Sialic Acid Linkage Detection.

We aimed to develop a high-throughput lectin assay with minimized background signals to investigate the interactions of lectins and sialic acid glycans, focusing on Prostate- Specific Antigen (PSA). High background signals resulting from nonspecific binding are a significant concern for microtiter plate-based Enzyme-Linked Lectin Sorbent Assays (ELISAs), as they can mask specific binding signals and cause false-positive results. In this study, we constructed an ELISA based on different washing step parameters, including the number of washing cycles, NaCl and Tween-20 concentrations, and the type of blocking agent and evaluated the effects on both specific and nonspecific binding signals. Furthermore, we performed a PSA binding assay using the optimized ELISA. The optimal washing parameters based on the highest specific binding signal proposed four cycles of washing steps using a washing buffer containing a high salt concentration (0.5 M NaCl) and mild detergent (0.05% Tween-20). The utilization of the optimized washing parameters in this assay was shown to be sufficient to obtain the optimal binding signals without the use of any blocking agent. Binding assays performed using the optimized ELISA revealed that the glycan of the PSA sample used in this study mainly consists of terminal α2,6-linked sialic acid, as strongly recognized by Sambucus nigra agglutinin (SNA) with a KD value of 12.38 nM. The ELISA reported in this study provides a simple yet sensitive assay for sialic acid linkage recognition.

Obtaining biologically active substances from Amaranthus caudatus L. seeds in one technological cycle.

Nowadays, amaranth is a valuable multipurpose crop and a source of a number of very important biologically active substances. The aim of this study was to develop a comprehensive scheme for obtaining fatty oil, triterpenoids and lectin from the seeds of Amaranthus caudatus L. in one technological cycle. Two variants of the lectin and triterpene compound purification method from amaranth seeds were tested. It was determined that the extraction of triterpene compounds should be carried out after purification of the lectin from degreased seeds. The rationality of this sequence of technological operations is explained by the lability of the lectin and the insolubility in water of triterpene compounds from amaranth seeds. The study also presents a scheme for obtaining squalene from amaranth oil by chromatography on silica gel and proposes a more effective affinity sorbent for purification of the lectin. The use of such a sorbent also opens up the possibility of preserving other water-soluble substances from amaranth seeds. The physicochemical characteristics and carbohydrate specificity of the lectin are described and new data on the results of the interaction of lectin with human and animal erythrocytes are given. The obtained results are discussed in the light of the complex use of raw materials.

Thermoresponsive Glycopolypeptide Containing Block Copolymers, Particle Formation, and Lectin Interaction.

Amphiphilic block copolymers with a thermoresponsive poly(N-isopropylacrylamide) block and a glycopeptide block are synthesized and particle formation as well as interaction of the glyco-corona with lectins is investigated. The synthetic route comprises the preparation of block copolymers by N-carboxyanhydride polymerization and subsequent deprotection to obtain pH- and thermoresponsive poly(l-glutamic acid)-b-poly(N-isopropylacrylamide) (pGA-b-pNIPAM), which is then further modified with different amino sugars by a versatile coupling method with 4-(4,6-dimethoxy-1,3,5-triazin-2-yl)-4-methylmorpholin-4-ium chloride (DMT-MM). The glycosylated pGA-b-pNIPAM block copolymers are investigated with regard to cloud point temperatures (Tcp ), particle size, and stability. The morphology of the particles is visualized using cryo-SEM. Zeta potential measurements are indicating that the saccharide moieties are located on the surface of the particles. This assumption is further substantiated by quantitative lectin interaction assays with nonaggregated and aggregated glycosylated pGA-b-pNIPAM. The interaction of the model lectin ConA with the block copolymers is independent of the degree of substitution in the nonaggregated state at room temperature. However, at 37°C, when particles of pGA-b-pNIPAM are present, the interaction becomes stronger with increasing degree of substitution. This interaction with lectins can be used for targeting saccharide-modified particles in drug delivery.

IN SILICO DETERMINATION OF THE PROBABLE TARGETS FOR LECTINS BINDING IN MIXED FEEDS

The study of the interaction of plant lectins with the target intestinal receptors of the weaning piglets by the in silico computer modelling method showed that the most probable targets for the lectin binding are the divalent metal transporter 1 (DMT1) and neutral amino acid transporter. Barley lectins have the greatest potential for interaction. Legume-type lectins and the OS9-like protein are the main types of reactive lectins. The addition of specific carbohydrates is the optimal method for neutralization of lectins.

Glycomimetic ligands block the interaction of SARS-CoV-2 spike protein with C-type lectin co-receptors.

The C-type lectin receptors DC-SIGN and L-SIGN bind to glycans on the SARS-CoV-2 spike glycoprotein and promote trans-infection of ACE2-expressing cells. We tested C2 triazole-modified mono- and pseudo-di-mannosides as inhibitors of DC/L-SIGN binding to a model mannosylated protein (Man-BSA) and to SARS-CoV2 spike, finding that they inhibit the interaction of both lectins with the spike glycoprotein in a Surface Plasmon Resonance (SPR) assay and are more potent than mannose by up to 36-fold (DC-SIGN) and 10-fold (L-SIGN). The molecules described here are the first known glycomimetic ligands of L-SIGN.

Polymer-tethered glyconanoparticle colourimetric biosensors for lectin binding: structural and experimental parameters to ensure a robust output.

Glycan-lectin interactions play essential roles in biology; as the site of attachment for pathogens, cell-cell communication, and as crucial players in the immune system. Identifying if a new glycan (natural or unnatural) binds a protein partner, or if a new protein (or mutant) binds a glycan remains a non-trivial problem, with few accessible or low-cost tools available. Micro-arrays allow for the interrogation of 100's of glycans but are not widely available in individual laboratories. Biophysical techniques such as isothermal titration calorimetry, surface plasmon resonance spectrometry, biolayer interferometry and nuclear magnetic resonance spectroscopy all provide detailed understanding of glycan binding but are relatively expensive. Glycosylated plasmonic nanoparticles based on gold cores with polymeric tethers have emerged as biosensors to detect glycan-protein binding, based on colourimetric (red to blue) outputs which can be easily interpreted by a simple UV-visible spectrometer or by eye. Despite the large number of reports there are no standard protocols for each system or recommended start points, to allow a new user to deploy this technology. Here we explore the key parameters of nanoparticle size, polymeric tether length and gold concentration to provide some guidelines for how polymer-tethered glycosylated gold nanoparticles can be used to probe a new glycan/protein interactions, with minimal optimisation barriers. This work aimed to remove the need to explore chemical and nanoparticle space and hence remove a barrier for other users when deploying this system. We show that the concentration of the gold core is crucial to balance strong responses versus false positives and recommend a gold core size and polymer tether length which balances sufficient colloidal stability and output. Whilst subtle differences between glycans/lectins will impact the outcomes, these parameters should enable a lab user to quickly evaluate binding using minimal quantities of the glycan and lectin, to select candidates for further study.

Increasing the biocompatibility of graphene-based hybrid nanostructures with glycopolymer

Hybrid nanostructures decorated with glycopolymers are appropriate for biomedical applications. In this paper, the results are obtained from nanographene (NG) decorated with glycoblock copolymer to increase their potential in use in therapies and in examining lectin interactions. A pyren-1-ylmethyl 4-cyano-4-((phenylcarbonothioyl)thio)pentanoate (CPADB-py) chain transfer agent was used in the synthesis of methyl methacrylate glycoblock copolymers (P2 and P3) by reversible addition-fragmentation chain transfer (RAFT) polymerization to adhere the polymer to the nanographene surface. Hybrid nanographenes (NG-1 and NG-2) were obtained by the non-covalent interaction of deprotected P2 and P3 with different fructopyranose groups (3-O-methacryloyl-1,2:4,5- di-O-isopropylidene-β-D-fructopyranose and 1-O-methacryloyl-2,3:4,5-di-O-isopropylidene-β-D-fructopyranose) in their backbones. Images obtained from transmission electron microscopy (TEM) of NG-1 and NG-2 show that glycoblock copolymer coating was performed homogeneously. Moreover, thermal gravimetric analysis (TGA) also confirmed a glycoblock copolymer coating of NG-1 and NG-2 by weight loss of 41% and 31%, respectively. In the last step of the study, the binding ability of glycoblock copolymers (P2-hyd and P3-hyd) with concanavalin A (ConA) lectin was investigated by a turbidimetric assay. Promising results were obtained from P3-hyd for the ConA interactions. Hence, this study may open a new avenue in the design of new multifunctional glyconanomaterials that show favorable binding properties with lectins.

Single-molecule imaging of glycan-lectin interactions on cells with Glyco-PAINT.

Most lectins bind carbohydrate ligands with relatively low affinity, making the identification of optimal ligands challenging. Here we introduce a point accumulation in nanoscale topography (PAINT) super-resolution microscopy method to capture weak glycan-lectin interactions at the single-molecule level in living cells (Glyco-PAINT). Glyco-PAINT exploits weak and reversible sugar binding to directly achieve single-molecule detection and quantification in cells and is used to establish the relative kon and koff rates of a synthesized library of carbohydrate-based probes, as well as the diffusion coefficient of the receptor-sugar complex. Uptake of ligands correlates with their binding affinity and residence time to establish structure-function relations for various synthetic glycans. We reveal how sugar multivalency and presentation geometry can be optimized for binding and internalization. Overall, Glyco-PAINT represents a powerful approach to study weak glycan-lectin interactions on the surface of living cells, one that can be potentially extended to a variety of lectin-sugar interactions.

Probing Multivalent Carbohydrate-Protein Interactions With On-Chip Synthesized Glycopeptides Using Different Functionalized Surfaces.

Multivalent ligand–protein interactions are a commonly employed approach by nature in many biological processes. Single glycan–protein interactions are often weak, but their affinity and specificity can be drastically enhanced by engaging multiple binding sites. Microarray technology allows for quick, parallel screening of such interactions. Yet, current glycan microarray methodologies usually neglect defined multivalent presentation. Our laser-based array technology allows for a flexible, cost-efficient, and rapid in situ chemical synthesis of peptide scaffolds directly on functionalized glass slides. Using copper(I)-catalyzed azide–alkyne cycloaddition, different monomer sugar azides were attached to the scaffolds, resulting in spatially defined multivalent glycopeptides on the solid support. Studying their interaction with several different lectins showed that not only the spatially defined sugar presentation, but also the surface functionalization and wettability, as well as accessibility and flexibility, play an essential role in such interactions. Therefore, different commercially available functionalized glass slides were equipped with a polyethylene glycol (PEG) linker to demonstrate its effect on glycan–lectin interactions. Moreover, different monomer sugar azides with and without an additional PEG-spacer were attached to the peptide scaffold to increase flexibility and thereby improve binding affinity. A variety of fluorescently labeled lectins were probed, indicating that different lectin–glycan pairs require different surface functionalization and spacers for enhanced binding. This approach allows for rapid screening and evaluation of spacing-, density-, ligand and surface-dependent parameters, to find optimal lectin binders.

Biofilm-Integrated Glycosylated Membrane for Biosuccinic Acid Production.

Biofilm-based cell-immobilized fermentation technology is regarded as the technique with the most potential for biobased product (chemicals, biofuelss materials, etc.) production in industry. Glycosylated membrane can mimic natural extracellular matrix (ECM) and improve cell adhesion and biofilm formation based on carbohydrate-microbial lectin interaction. Here, we applied glycosylated membrane with rhamnose modified surface for constructing Actinobacillus succinogenes biofilm and producing biosuccinic acid. Polymer hollow fiber (PHF) membrane surface was first modified by glycosylation based on physical adsorption approach. The approach is simple, green, and suitable for scale-amplification. Then, the microbial biofilm formed dramatically on the modified membrane surface. And for subsequent biosuccinic acid production, the maximum titer of succinic acid reached 67.3 g/L, and the yield was 0.82 g/g. Compared with free cell fermentation, the titer and yield increased by 18% and 9% in this biofilm-based cell-immobilized fermentation system, respectively. Importantly, the production efficiency of biosuccinic acid increased obviously for subsequent biofilm-based cell-immobilized fermentation. In addition, the biofilm-integrated glycosylated membrane showed high reusability for succinic acid production. This result is important for developing biofilms for a wide range of applications in bioproduct (chemicals, biofuels, materials, etc.) production.

Dynamic self-assembly of mannosylated-calix[4]arene into micelles for the delivery of hydrophobic drugs

Carbohydrate–lectin interactions and glycol-molecule-driven self-assembly are powerful yet challenging strategies to create supramolecular nanostructures for biomedical applications. Herein, we develop a modular approach of micellization with a small molecular mannosylated-calix[4]arene synthetic core, CA4-Man3, to generate nano-micelles, CA4-Man3-NPs, which can target cancer cell surface receptors and facilitate the delivery of hydrophobic cargo. The oligomeric nature of the calix[4]arene enables the dynamic self-assembly of calix[4]arene (CA4), where an amphiphile, functionalized with mannose units (CA-glycoconjugates) in the upper rim and alkylated lower rim, afforded the CA4-Man3-NPs in a controllable manner. The presence of thiourea units between calixarene and tri-mannose moiety facilitated the formation of a stable core with bidentate hydrogen bonds, which in turn promoted mannose receptor targeted uptake and helped in the intracellular pH-responsive release of antineoplastic doxorubicin (Dox). Physiochemical features including the stability of the nanomicelle could circumvent the undesirable leakage of the cargoes, ensuring maximum therapeutic output with minimum off-targeted toxicity. Most importantly, surface-enhanced Raman scattering (SERS) was utilized for the first time to evaluate the critical micelle concentration during the formation, cellular uptake and intracellular drug release. The present study not only provides an architectural design of a new class of organic small molecular nanomicelles but also unveils a robust self-assembly approach that paves the way for the delivery of a wide range of hydrophobic chemotherapeutic drugs.

Glycan-Lectin Interactions in Cancer and Viral Infections and How to Disrupt Them.

Glycan–lectin interactions play an essential role in different cellular processes. One of their main functions is involvement in the immune response to pathogens or inflammation. However, cancer cells and viruses have adapted to avail themselves of these interactions. By displaying specific glycosylation structures, they are able to bind to lectins, thus promoting pathogenesis. While glycan–lectin interactions promote tumor progression, metastasis, and/or chemoresistance in cancer, in viral infections they are important for viral entry, release, and/or immune escape. For several years now, a growing number of investigations have been devoted to clarifying the role of glycan–lectin interactions in cancer and viral infections. Various overviews have already summarized and highlighted their findings. In this review, we consider the interactions of the lectins MGL, DC-SIGN, selectins, and galectins in both cancer and viral infections together. A possible transfer of ways to target and disrupt them might lead to new therapeutic approaches in different pathological backgrounds.

Surface Density of Ligands Controls In-Plane and Aggregative Modes of Multivalent Glycovesicle-Lectin Recognitions.

Glycovesicles are ideal tools to delineate finer mechanisms of the interactions at the biological cell membranes. Multivalency forms the basis which, in turn, should surpass more than one mechanism in order to maintain multiple roles that the ligand-lectin interactions encounter. Ligand densities hold a prime control to attenuate the interactions. In the present study, mannose trisaccharide interacting with a cognate receptor, namely, Con A, is assessed at the vesicle surface. Synthetic (1→3)(1→6)-branched mannose trisaccharides tethered with a diacetylene monomer and glycovesicles of varying sugar densities were prepared. The polydiacetylene vesicles were prepared by maintaining uniform lipid concentrations. The interactions of the glycovesicles with the lectin were probed through dynamic light scattering and UV-Vis spectroscopy techniques. Binding efficacies were assessed by surface plasmon resonance. Aggregative and in-plane modes of interactions show ligand-density dependence at the vesicle surface. Vesicles with sparsely populated ligands engage lectin in an aggregative mode (trans-), leading to a cross-linked complex formation. Whereas glycovesicles embedded with dense ligands engage lectin interaction in an in-plane mode intramolecularly (cis-). Sub-nanomolar dissociation constants govern the intramolecular interaction occurring within the plane of the vesicle, and are more efficacious than the aggregative intermolecular interactions.

Facile synthesis of Antibacterial, Biocompatible, quaternized Poly(ionic liquid)s with pendant saccharides

Glycopolymer has been developed in bactericidal applications, but the traditional synthesis, such as click chemistry, needs poly-step reactions and complicated processes. Herein, incorporating the glyco-units into the polymers by quaternization has been exploited to give a facile strategy by Copper-mediated reversible deactivation radical polymerization (Cu(0)-RDRP) to prepare quaternized poly(ionic liquid)s (PILs) with pendant saccharide. The obtained PILs have the suitable property of killing typical Gram-negative Escherichia coli and Gram-positive Staphylococcus aureus. Simultaneously, they perform the lower hemolytic rate of blood cells, higher selectivity index against bacteria, and higher affinity with Concanavalin A (ConA) than those quaternized by bromohydrin at the same quaternization degree. This result demonstrated that the introduced saccharide units, such as glucose and mannose, could maintain the electrostatic interaction to kill bacteria, perform lectin recognition behavior and interaction with ConA, and relatively harmlessness against red blood cells. Moreover, the sugar-containing PILs became insoluble and still antibacterial after anion exchange reaction. These new findings illuminated that such quaternized antibacterial agents with saccharide units that are easy-to-prepare, low cytotoxic could pave the way for further water disinfectant and pathogen control application.

Increasing the biocompatibility of graphene-based hybrid nanostructures with glycopolymer.

Hybrid nanostructures decorated with glycopolymers are appropriate for biomedical applications. In this paper, the results are obtained from nanographene (NG) decorated with glycoblock copolymer to increase their potential in use in therapies and in examining lectin interactions. A pyren-1-ylmethyl 4-cyano-4-((phenylcarbonothioyl)thio)pentanoate (CPADB-py) chain transfer agent was used in the synthesis of methyl methacrylate glycoblock copolymers (P2 and P3) by reversible addition-fragmentation chain transfer (RAFT) polymerization to adhere the polymer to the nanographene surface. Hybrid nanographenes (NG-1 and NG-2) were obtained by the non-covalent interaction of deprotected P2 and P3 with different fructopyranose groups (3-O-methacryloyl-1,2:4,5-di-O-isopropylidene-β-D-fructopyranose and 1-O-methacryloyl-2,3:4,5-di-O-isopropylidene-β-D-fructopyranose) in their backbones. Images obtained from transmission electron microscopy (TEM) of NG-1 and NG-2 show that glycoblock copolymer coating was performed homogeneously. Moreover, thermal gravimetric analysis (TGA) also confirmed a glycoblock copolymer coating of NG-1 and NG-2 by weight loss of 41% and 31%, respectively. In the last step of the study, the binding ability of glycoblock copolymers (P2-hyd and P3-hyd) with concanavalin A (ConA) lectin was investigated by a turbidimetric assay. Promising results were obtained from P3-hyd for the ConA interactions. Hence, this study may open a new avenue in the design of new multifunctional glyconanomaterials that show favorable binding properties with lectins.