Synthetic glycans are no longer viewed simply as reagents for proof-of-concept cell assays but are now fully integrated as therapeutic entities that are defining biopharma approaches to vaccines, monoclonal antibodies and targeted protein modifiers. As their structures can be defined at the single-atom level of isotopic substitution, synthetic glycans also allow structure–activity relationships to be disentangled that are otherwise masked by the micro-heterogeneity of material that is isolated from natural sources. The same batch can also be sequentially re-purposed to GMP toxicology, bio-distribution and phase-one dosing without re-qualification, reducing development timelines and regulatory risk. At the same time, the ability to install non-natural linkages or backbone epimers provides intellectual-property space that is unavailable to harvested polysaccharides, leading to commercial exclusivity beyond the life of a patent. As a result, synthetic glycans now find applications throughout the biopharma value chain, from early target validation all the way through to lot-release analytics.
An interesting feature of carbohydrate vaccines is that they change the quality of the immune response (T cell independent response to polysaccharide to strong memory bearing T cell dependent response) by covalently linking the glycan to a carrier that can elicit an immune response. The advantage of synthetic accessibility is that the medicinal chemist can trim or decorate these antigens so that only the protective epitope is displayed and no cross reactive decoy antigens are present to confuse specificity and sometimes cause auto-immune like effects. The pure nature of the final product also allows the CMC portions of the registration package to be easier because it boils down to a single entity rather than a population. But perhaps of equal importance is the development of scalable chemo-enzymatic synthetic routes that can provide gram to kilogram amounts of highly pure complex oligosaccharides that can be used at the high dose levels needed in pre-clinical testing as well as the subsequent adjuvantation studies thus removing the supply issue that once placed glycan vaccines in the orphans' corner.
Fig. 1 Overview of the glycoconjugate vaccine synthesis technologies.1,5
Chemical conjugation of a glycan hapten to a protein carrier reroutes antigen trafficking in the antigen-presenting cell (APC), for example, a dendritic cell (DC). The hapten is sensed by C-type lectin receptors (CLR) DC-SIGN or Mincle on the cell surface, while the carrier supplies proteolytic peptides that are loaded on to MHC-II molecules, thereby eliciting CD4+ T-cell help. The interaction between APCs and T-cells relies on linker length modulation together with anomeric configuration adjustments and changes in hapten density since short and rigid spacers facilitate receptor clustering and pro-inflammatory cytokine release while long flexible tethers reduce steric hindrance and enhance peptide processing. The angle of the glycan to the surface of the carrier also affects the antibody epitope focus of the immune response; head-to-tail conjugation for example can expose the inner core sugars of the glycan that are often masked, shifting the immune response away from the predominant end-group motif. Additionally, synthetic chemistry routes allow for the non-natural amino acids to be built into the carrier so that bioconjugation chemistry can be site-selective and thus avoid the heterogeneous lysine conjugation of first generation vaccines. This results in more batch-to-batch consistency of epitope density and ensures that every new manufacturing campaign does not inadvertently alter the fine specificity of the elicited antibodies. Lastly, co-formulations can be made in which the glycoconjugate and a pattern-recognition-receptor (PRR) agonist are conjugated to the same nanoparticle platform, such that innate activation and antigen presentation are synchronous and result in a higher magnitude and more durable germinal-center (GC) reaction.
Pathogens are known to embellish their surfaces with glycans that mimic those found on host cells, or ones that closely resemble them, as this lessens immune recognition by molecular mimicry. The opposite strategy can be pursued synthetically, by incorporating subtle stereochemical or linkage differences that maintain affinity for protective antibodies, but which fall outside the permissive threshold for self-tolerance. Thus, a host-type β1→6 linkage can be replaced by a β1→3 junction, generating a neo-epitope that is recognised as foreign, while still eliciting cross-reactive antibodies that can neutralise the wild-type pathogen. Such "micro-mimics" can be generated in parallel by selective deprotection/re-glycosylation of a common core, after which multiple antigen variants can be screened for optimal immunogenicity. The molecules are homogeneous, and therefore structure–activity relationships can be determined at single-residue resolution, which can inform iterative refinements that would be difficult or impossible with naturally heterogeneous isolates. Moreover, synthetic glycans can be functionalized with latent handles (e.g. azide, alkyne or thiol) for click-chemistry conjugation to virus-like particles or lipid bilayers, thus creating multivalent constructs that can more closely mimic the high glycan density on the surfaces of microbes. Multivalent constructs produce antibodies that exhibit increased avidity when compared to monovalent conjugates despite having identical total carbohydrate doses. Finally, precision synthesis allows incorporation of isotopic labels (2H, 13C, 15N), that can serve as internal standards during later pharmacokinetic analysis, enabling the same molecular entity used for immunisation to be tracked quantitatively in vivo, without the need for heterologous tracers.
Recent progress in chemo-enzymatic cascades, which combine the regioselectivity of glycosyltransferases with the scalability of chemical glycosylation, have opened up the possibility of manufacturing complex antigens like fully sulphated meningococcal serogroup W capsules or branched fungal β-glucans, which were previously unavailable in homogeneous form. Enzymes used for this purpose can be immobilised on reusable resins, permitting flow-through synthesis with greatly reduced catalyst consumption and simplified work-up. In parallel, lipidated glycan conjugates have been developed that self-assemble into nanoparticles, bypassing the need for an exogenous carrier protein and thereby avoiding issues with increased formulation complexity and anti-carrier immunity. An orthogonal approach involves using mRNA templates to encode glycosyltransferases for in-vivo expression within the vaccinated host, such that the desired glycan antigen can be assembled on a co-administered scaffold protein inside dendritic cells with physiological conjugation but minimal manufacturing steps. Progress in analytical speed, such as on-line LC–MS reaction monitoring of glycosylation reactions, is now delivering real-time feedback and compressing optimization cycles from weeks to hours. Lastly, the deployment of machine-learning algorithms to glycan micro-array datasets enables identification of the minimal epitope necessary for the elicitation of broadly neutralizing antibodies, focusing synthetic efforts on the smallest (i.e., lowest cost) carbohydrate structure with protective potential. Cumulatively, these developments are shifting the positioning of glycan vaccines from specialist products against niche bacterial pathogens to platform technologies with viral, fungal and even oncological indications.
The field of antibody development has shifted its perspective on Fc glycosylation from a mere post-translational modification to a critical control element that adjusts antibody longevity and function effectiveness while influencing safety margins in certain therapeutic contexts. The oligosaccharide repertoire can be 'programmed' using cell-line genetics, media supplements or even in-vitro enzymatic remodeling. As a result, therapeutic developers often iterate glycoform profiles in parallel to CDR optimisation with glycan composition considered an additional degree of freedom in antibody design. The outcome is a single molecule which can be tuned for maximum tumour cell deletion, silent receptor blockade or even enhanced circulation simply by tweaking the composition of a seven sugar core far removed from the antigen binding cleft. Glycan metrics are also increasingly regarded as critical quality attributes by regulatory agencies, making their control important not only for first in human studies but also commercial consistency.
The N-glycan hidden between the two CH2 domains can also act as a conformational lubricant: its presence locks the structure in the open form that is required for FcγR binding, and its removal collapses the pocket and abolishes effector function. By deleting the fucosyltransferase gene or adding a fucose scavenger to the feed we can achieve Afucosylation which removes the steric shield blocking FcγRIIIa access resulting in tighter binding and enhanced ADCC without any sequence changes. On the other hand, increasing terminal sialic acid by over-expression of β-galactoside α2,6-sialyltransferase skews signalling toward the inhibitory FcγRIIb, and is part of the strategy for engineering anti-inflammatory antibodies. Non-natural monosaccharides can be installed in place of natural sugars using chemo-enzymatic approaches; because they are not recognized by in-vivo cleavage enzymes they can effectively fix the molecule in a specific activity state for weeks. The chemistry of the linker between monosaccharides is important too: a short rigid glycosidic arm limits the mobility of the oligosaccharide and can enhance complement activation, while a long PEG-like spacer can mute cytokine release through limiting receptor clustering. Comparing crystal structures overlays these modest glycan perturbations within less than an ångström on the lower hinge, but that tiny shift maps through to quantifiable differences in cytotoxic potency, explaining why glycan engineering is now pursued with the same vigour as affinity maturation.
Glycan modification extends serum half-life by hiding the recognition motifs that trigger pinocytosis and lysosomal targeting. Terminal galactose enrichment accelerates clearance through the asialoglycoprotein receptor, so its targeted removal (or replacement with N-acetylglucosamine) can extend half-life and allow for less-frequent dosing. Core α1,3-fucose presence induces a hydrophobic patch that may be sensitive to aggregation during agitation; enzymatic removal increases the melting temperature of the CH2 domain and reduces apparent aggregation during long-term storage. The propensity for oxidative degradation is also modulated by glycan shielding: a bisecting GlcNAc sterically prevents solvent access to the pair of methionines flanking the N-glycan sequon, precluding the build-up of sulphoxide variants that would otherwise form under photo- or metal-catalysed stress. For bispecific molecules, each arm can be differentially glycosylated to drive one Fc towards rapid clearance while retaining the other, creating a kinetic "detuning" that is believed to attenuate on-target, off-tumour toxicities. Finally, the addition of a second N-glycan to the hinge region (previously deemed infeasible because of interference with disulphide formation) has been demonstrated to confer increased resistance to papain-like proteases, a feature especially desirable for subcutaneous products where tissue proteases are prevalent.
Afucosylated anti-CD20 antibodies produced in FUT8-deficient hosts were shown to preferentially deplete B cells in refractory lymphoma at the same dose as the affinity matured variants. In another example, an anti-HER2 molecule whose Fc was hyper-sialylated using fed-batch addition of ManNAc, experienced diminished infusion-related toxicity, while maintaining tumour growth inhibition. The hyper-sialylation in this case represents immune dampening through glycan modification without loss of efficacy. A bispecific T-cell engager (BiTE) to a solid tumour antigen has also been engineered with a mosaic glycan landscape where one arm was designed to have a high mannose glycan profile for fast systemic clearance, while the other arm was modified with a sialylated complex-type glycan that accumulates in the tumor bed, producing a gradient in local concentration and therapeutic index. More recently, a complement-activating antibody against a viral envelope protein was modified to have a galactose-extended Fc. The emerging glycoform attached itself to C1q which enabled powerful viral lysis at serum levels less than those necessary for neutralisation by itself. In each of these examples, the common element is the substitution of an empirical glycoform mixture with well-defined oligosaccharide profiles whose functional outputs are predictable, scalable and designed to match the desired clinical endpoint.
Diagnostic technologies are following up on the clinical success of carbohydrate-focused analysis beyond the traditional set of enzyme-deficiency disorders. In particular, cancer, infection/inflammation signals are targets. The impetus for this arises from two realizations. First, the biosynthesis of glycans is highly sensitive to microenvironmental stimuli and, secondly, that high-affinity reagents (plant lectins, human antibodies, or synthetic aptamers) can now be generated on demand. Since glyco-epitopes are often presented on the host–pathogen interface or the surface of circulating exosomes, they generate signals that are anatomically specific, quantifiable, and, most importantly, discernable in very small sample volumes. Triangulated data generated when the same glycan signature is interrogated by orthogonal platforms (micro-arrays for screening, LC–MS for confirmation, and electrochemical biosensors for point-of-need testing) meets both discovery and regulatory expectations, and does not require the repetitive re-validation associated with a single-platform workflow.
Single slide high-density glycan micro-arrays immobilise hundreds of different oligosaccharide structures to enable multiple biological samples (including sera, saliva, cell lysates and culture supernatants) to be tested for binding specificity in one incubation process. The read-out is usually fluorescence, but chemiluminescent or plasmonic detection can be substituted when autofluorescence is problematic. Since the printed sequences are synthetic, each spot is chemically defined, and batch-to-batch variability is not a concern as it is with classical ELISA plates coated with natural extracts. Pathogen-induced antibodies often recognise carbohydrate motifs that are either absent or cryptic in the host, and so arrays can therefore reveal serological signatures of infection long before protein-based biomarkers reach detectable titres. In oncology, aberrant fucosylation or sialylation patterns on secreted glycoproteins generate auto-antibody responses which can be captured by array screening, providing a route to early detection that complements imaging or nucleic-acid liquid biopsy. Data analysis pipelines normalise spot intensities against internal control glycans, apply hierarchical clustering to identify disease-specific reactivity hotspots and export the resulting patterns as heat-maps compatible with machine-learning classifiers. Crucially, the same array can be re-scanned after enzymatic treatment with exoglycosidases or sulfatases, so the precise epitope boundary can be trimmed and re-defined without fabricating a new chip. When archived sera from longitudinal cohorts are profiled retrospectively, arrays can reconstruct temporal trajectories of glyco-immunity and reveal whether a patient seroconverted months before clinical symptoms appeared – information that is invaluable for validating the predictive value of emerging carbohydrate biomarkers.
Cancer cells alter glycosyltransferase expression to promote glycan biosynthetic branches that mediate immune evasion and metastasis. These changes are mirrored in the serum N-glycome where, for example, tri-antennary structures capped with α2,3-linked sialic acid have been consistently reported in late-stage carcinomas and core-fucosylated bi-antennary glycans enriched in early-stage lesions. Mass-spectrometric relative quantification, facilitated by isotopic labelling, can be used to measure these changes across hundreds or thousands of patient samples, providing receiver-operating curves that frequently exceed traditional protein biomarkers like CEA or CA19-9. Viral surface glycoproteins of enveloped viruses are by definition the primary antigenic target of a host response. Glycans on these proteins, however, also function as pathogen-associated molecular patterns. Antiviral antibodies targeting viral high-mannose patches or Lewis-type antigens can therefore be detected irrespective of viral load and have been used to diagnose infection for purposes of serosurveillance with emerging coronaviruses or arthropod-borne flaviviruses. Lyophilised assay formats are possible because glycan antigens are chemically stable and non-infectious, and multiplexed lectin magnetic-bead assays are able to survey a much wider array of glyco-epitopes in a single tube, while retaining compatibility with 96-well plate readers that are already in use in clinical labs. The discovery pipeline no longer stops at statistical significance: candidate glycan signatures are now immediately transferred to orthogonal platforms such as LC–MS or capillary electrophoresis for confirmatory validation, so that only the most robust and reproducible markers make it into diagnostic kits.
A research glycan assay can be reformatted for CE-marking or FDA clearance by streamlining reagent handling and data analysis steps to reduce run time and user error. Lyophilised cocktails of lectins or fluorescently labelled antibodies can be placed into one bar-coded vial which is rehydrated with a set volume of patient sample, standardising dilutions and avoiding pipetting steps. Patient sample can be captured in microfluidic cartridges with a built-in glycan-functionalised gold electrode which provide an amperometric readout within minutes and use a volume of sample several orders of magnitude smaller than a 96-well plate. On-chip calibration with internal standards of known glycan concentration means every run on a cartridge is self-normalised and external standard curves are not required. A server that is accessible through cloud connectivity can receive raw current responses to provide machine-learning based probability scores rather than raw intensity measures, protecting clinicians from unit conversions or manual cut-off determinations. Packaging must be designed for the intended storage conditions. Trehalose matrices and argon-filled pouches can maintain lectin activity for months at tropical temperatures and colourimetric readouts substituting for laboratory-based fluorimeters can be photographed with smartphone cameras. Regulatory data requirements include stability studies showing<10 % signal drift across freeze-thaw cycles, panels showing negligible cross-reactivity with rheumatoid factor or heterophilic antibodies, and parallel testing against a predicate assay to demonstrate equivalence. Following clearance, the same kit platform can be reloaded with new glycan specificities simply by changing the capture surface, providing a future-proof architecture to rapidly incorporate emerging pathogens or new glyco-phenotypes on the same device without re-engineering.
Carbohydrate-based targeting approaches are also making headway. These are based on the often high density of carbohydrate ligands and their soluble receptors on the cell surface for spatial and temporal control of biodistribution. By adjusting glycan density and linkage topology and anomeric orientation, receptors can be engaged via avidity or monovalently in order to modulate the activation thresholds of endocytosis, transcytosis or lysosomal escape. The glycan platform itself can simultaneously hide a hydrophobic drug from clearance and serve as a synthetic handle for post-production modification thus blurring the lines between delivery vehicle and active moiety. As safety data for synthetic oligosaccharides are being accumulated by regulatory agencies, glycan-mediated delivery approaches are progressing from proof-of-concept exercises into broad pipelines targeting cancer, auto-immune and infectious disease.
Site-specific conjugation of a therapeutic payload to a carbohydrate ligand is first based on an orthogonal coupling strategy that is compatible with aqueous buffers to preserve bioactivity. Reductive amination between a reducing sugar and the primary amine of a drug provides a stable secondary amine but the reaction is reversible in low pH conditions and the payload can thus be released in late endosomes. Click chemistry instead leverages the bio-orthogonality of azide–alkyne cycloaddition, which can be used to form the conjugate under physiological conditions in the absence of protecting groups. The anomeric position is often favored because it projects the payload away from the binding face, thus avoiding interference with receptor affinity. Remote hydroxyl groups can alternatively be activated with sulfonate esters to form branching points to append multiple drugs or imaging reporters. The spatial separation of glycan and cargo is a key parameter: short linkers allow optimal receptor clustering but increase the risk of off-target uptake by scavenger receptors; long and flexible tethers can circumvent steric hindrance but may be more susceptible to premature hydrolysis. Chemo-enzymatic methods make use of bacterial glycosyltransferases to transfer non-natural monosaccharides that have latent chemical handles for subsequent toxin attachment under mild conditions. Once prepared, the glyco-drug can be purified by hydrophilic-interaction chromatography based on the hydrophilic contribution of the sugar, which can help to resolve hydrophobic payload contaminants. In the body, the conjugate traverses galectin lattices lining the vascular endothelium and co-opts natural carbohydrate–carbohydrate interactions to target tissue beds that remain elusive to naked small molecules. The same glycan can also be recognized by inhibitory and activating receptors; thus, subtle variations in linkage geometry or peripheral decoration can switch the pharmacological outcome from immune activation to silent delivery and act as a tunable rheostat for therapeutic index optimization.
Drug-encapsulating nanoparticles functionalized with surface-displayed glycans combine the colloidal protection of a nanocarrier with the specific recognition offered by carbohydrate–lectin interactions. The core can be built from biodegradable polyesters or, depending on the required timing with the pathology indication, inorganic silica. Surface glycan density is adjusted by either co-polymerizing a sugar-containing monomer during nanoprecipitation or by post-inserting lipidated oligosaccharides in pre-formed vesicles; in the latter case, it is possible to switch on demand the targeting profile without having to redesign the whole particle. Dendritic cell lectins are preferentially engaged by high mannose clusters, thus driving vaccines to professional antigen-presenting cells, whereas Lewis-type epitopes bind to E-selectin displayed on inflamed endothelium, enabling site-specific delivery of anti-inflammatory drugs. The size is adjusted so that they are large enough to escape renal filtration but small enough to avoid splenic clearance, and zeta potential is modulated by adding sialic acid residues that impart an electrostatic shielding to avoid serum protein adsorption. According to cryo-electron tomography, glycan chains display a mushroom-to-brush conformational transition as a function of surface density, a change that is associated with increased avidity but reduced cellular uptake and therefore should be optimized kinetically rather than at equilibrium. Multivalent display can itself induce receptor clustering and trigger signalling, even in the absence of a pharmacological cargo. It is therefore essential that blank particles are thoroughly screened for immune activation in pre-clinical safety testing. Finally, the same glycan shell can be cross-linked with boronic acid or phenylboronate derivatives to form a dynamic covalent network that dissociates in response to acidic pH or cis-diol competition. This provides an internal release trigger that is only activated once the particle has reached the target organelle.
Fig. 2 The common forms of glycan-based scaffolds and targeted delivery of drugs.2,5
Glycan density affects not only targeting selectivity, but also the kinetics of payload release from the carrier or conjugate. Enzyme-cleavable linkers have been designed to incorporate β-galactoside or α-mannoside bonds which are stable in the circulation, but are cleaved by lysosomal glycosidases to link release to cellular internalization. In contrast, boronate esters formed between a glycan cis-diol and a boronic acid-modified drug are dissociated by pH-sensitive kinetics that provide a slow diffusion gradient for long-term maintenance of local drug concentrations. When the glycan is immobilized in a hydrogel instead of as a surface ligand, swelling behavior can be tuned by ionic strength and by competitive chelation of calcium ions that cross-link glucuronic acid residues, and so convert extracellular changes in electrolytes into macroscopic payload release. Pharmacokinetic modelling has shown that glycan-mediated targeting often reduces initial distribution half-life due to rapid receptor-mediated uptake, but extends total drug exposure by slowing endosomal release and renal clearance of the high-molecular-weight conjugate. The same models predict that this dose-sparing effect only becomes significant when the targeted receptor is expressed on a relatively small cell population, which is typical for tumor-initiating cells or tissue-resident macrophages. Glycan conjugates can also be designed to undergo orthogonal clearance pathways: high-mannose variants are rapidly sequestered by liver Kupffer cells, while sialylated counterparts recycle back into the circulation via the neonatal Fc receptor, providing a rational basis for developing combination regimens that leverage divergent biodistribution profiles. By considering these parameters in physiologically based pharmacokinetic simulations, developers can more accurately predict human doses from pre-clinical data with less iterative animal testing, in line with ethical efforts to reduce, refine and replace in-vivo studies.
The carbohydrate community is moving from a position of supportive service speciality to one of key enabling pillar in the next wave of biomanufacturing, driven by a confluence of advancements in automated synthesis, high resolution analytics, and data analytics for process control. Instead of using glycans as unreactive excipients, they are now used to their full chemical versatility to make real-time decisions inside cells - e.g. instructing the differentiation of stem-cells, shielding viral vectors from the innate immune system, or controlling multivalent interactions with the immune system. The same process development platforms that can produce gram scale quantities of clinical-grade oligosaccharides can be repurposed within days to provide a patient-specific sequence tailored to a patient's genomic or glycomic profile, increasingly blurring the lines between one-off custom synthesis and commodity manufacturing. As sustainability becomes an increasingly important metric, these bio-catalytic glyco-syntheses performed in water and at ambient pressure offer a low-carbon footprint alternative to small molecule organic chemistry, and can enable glycans to be both functional and green technology enablers.
Precision glycosylation is also beginning to be recognized as a deterministic regulator of stem-cell identity. Synthetic oligosaccharides on hydrogel scaffolds recapitulate the glyco-code of native ECM in order to bias pluripotent cells toward lineage-specific fates without the addition of recombinant cytokines. For example, immobilized Lewis-type epitopes drive endothelial commitment, whereas immobilized high-mannose clusters promote chondrogenic condensation. The same logic is applied in the ex-vivo expansion of T-cells, where culture surfaces decorated with sialylated lacNAc maintain the naïve phenotype longer, reducing exhaustion upon differentiation and increasing potency of engraftment. Viral and non-viral gene-therapy vectors are now being cloaked with custom glycan shields to avoid pre-existing antibodies; afucosylated high-mannose envelopes drive transduction of dendritic cells to amplify vaccine responses. Finally, 3D bioprinting formulations now incorporate glycosaminoglycan mimics that can be enzymatically remodelled after implantation to allow the construct to mature in parallel with host integration. Converging on these points, synthetic glycans will soon be considered instructive components instead of inert scaffolds in regenerative medicine workflows.
Variability in glycosyltransferase genes between patients leads to quantifiable differences in the glycosylation of drug receptors that in turn change pharmacokinetic and immunogenic profiles. Synthetic glycan panels can act as companion diagnostics: application of a drop of blood to a microfluidic lectin array enables stratification of patients into high- or low-fucosylation phenotypes that in turn guide treatment frequency (weekly or monthly) for a given biologic. Oncologists are leading the way with efforts to predict in patients with solid tumors those who will benefit from afucosylated antibodies that depend on FcγRIIIa binding. Similarly, tumor-associated glycan antigens are being included in personalized cancer vaccines: neo-glyco-epitopes discovered by glycoproteomic interrogation of a patient's own lesion are synthesized, conjugated to an immunogenic carrier and returned to clinic within weeks to fit the short timelines that are now expected in precision immuno-oncology. Outside of cancer, glycosylation patterns in maternal plasma can correlate with the risk of pre-eclampsia and offer another non-invasive option for precision medicine in obstetrics. These correlations are refined by cloud-based algorithms that incorporate new patient data as they are uploaded, ensuring glycan-based decision thresholds are grounded in real-world evidence and not locked in at the time of approval.
Expanding uses of defined glycans in cosmetics, agritech, and functional foods are broadening revenue streams for early-stage companies so they are not reliant on a single market. CDOs that previously only focused on protein manufacture are investing in glycan production capabilities to provide a one-stop-shop to their customers that services the entire value-chain from gene to glycan to GMP material. Organizations like the Public-private Consortium for Functional Glycomics are working on standardization efforts in carbohydrate analysis that are open-source databases of fragmentation spectra to make entry more accessible for smaller companies, and to help unify regulatory demands. Collaborations are also forming on the sustainability front, as glyco-enzymatic approaches to chemical synthesis can remove the need for heavy-metal catalysts and allow companies to meet sustainability or carbon-reduction goals. Glycan-based biomanufacturing processes are also potentially viable for green loans and other sustainable financial products. Teams of chemists, biologists, and data scientists are forming collaborations on hybrid approaches to synthesize glycans. These collaborations can leverage AI-assisted retrosynthesis to identify glycan synthesis routes that are both synthetically accessible and cost-effective given current raw material costs. For example, a shifting reimbursement model to one that is focused on patient outcomes may open opportunities for glycans to find utility based on the improved clinical results it can offer, and with an IP environment that is more amenable to licensing over litigation.
From early-stage discovery to advanced therapeutic development, our glycan research team partners with scientists and biopharma innovators to accelerate progress in synthetic glycan applications. We combine deep expertise in glycoscience with scalable technology to translate complex carbohydrate chemistry into real-world biomedical solutions.
We understand the challenges of developing glycan-based therapeutics, vaccines, and diagnostics. Our multidisciplinary team of chemists, biologists, and analytical specialists works side-by-side with you to co-design experiments, optimize synthesis routes, and characterize novel glycans with precision.
Our services go beyond synthesis. We offer custom glycan production, HPLC and LC-MS analysis, and structural validation under one roof—ensuring seamless coordination and data consistency. This integrated approach reduces development time and improves reproducibility for complex biopharma projects.
We collaborate with research teams and biotechnology companies worldwide, delivering synthetic glycan solutions tailored to diverse therapeutic pipelines. Our flexible models-ranging from technical consultation to full-service project execution-ensure that your research receives the depth, rigor, and agility it deserves.
Accelerate your glycan innovation today. Contact our Glycan Research Team to discuss your project goals or request a partnership proposal.
1. How are synthetic glycans used in biopharma research?
They're applied in vaccine development, antibody engineering, diagnostic assays, and drug delivery system design.
2. Why use synthetic instead of natural glycans?
Synthetic glycans offer precise control over structure and function, ensuring consistency and scalability for regulated applications.
3. What role do glycans play in antibody optimization?
Glycan engineering in the Fc region improves antibody stability, efficacy, and immune effector functions.
4. Are synthetic glycans relevant for diagnostics?
Yes. They serve as well-defined standards and capture agents for biomarker detection and disease profiling.
5. Can I collaborate with experts on glycan-based projects?
Definitely. Our glycan research team partners with biopharma and academic labs to co-develop innovative glycan-based solutions.
References
