{"doi":"10.1002/adhm.202200096","title":"Medical Applications of Glycomaterials","abstract":"Carbohydrates are the most abundant organic molecules on Earth. Chains of covalently-linked carbohydrates, or glycans, decorate the surfaces of cells found throughout the various kingdoms of life as well as viruses, and are abundant within the extracellular matrices of multicellular organisms. In human biology, glycans participate in nearly all aspects of life, as exemplified by numerous disorders associated with deficient glycan synthesis. In general, glycans can be subdivided into long, often repeated structures, referred to as polysaccharides, or short, complex structures, referred to as oligosaccharides. Polysaccharides are key structural components of plant cell walls and vegetable fibers (cellulose), arthropod exoskeletons (chitin), bacterial biofilms (polysaccharide intercellular adhesin), and mammalian tissues (glycosaminoglycans), among others. For example, the glycosaminoglycan known as hyaluronic acid (HA) is abundant in articular cartilage and synovial fluid, where it acts as a lubricant, shock absorber, regulator of water content, and contact site for cell adhesion. Oligosaccharides, on the other hand, are generally found attached to proteins (i.e., glycoproteins) or lipids (i.e., glycolipids), where they impact the structure, solubility, and stability of the carrier molecule onto which they are attached. Oligosaccharides are also key mediators of cell-to-cell communication through their ability to bind to a broad class of soluble and membrane-anchored proteins known as lectins. The diverse biological activity of oligosaccharides arises from their extraordinary chemical complexity — the 10 different monosaccharides found in humans could give rise to ∼1010 different hexasaccharide glycans by way of linkages formed via the anomeric carbons or various hydroxyls, which leads to different linear and branched structures, as well as the α and β stereochemistry of the glycosidic bond. Additional glycan modifications, such as methylation, sulfation, phosphorylation, and acetylation, broaden this chemical diversity even further. Naturally derived polysaccharides have a long and well-established history as biomaterials for medical applications, while oligosaccharides now receive considerable attention as active components of biopharmaceuticals. A new frontier of glycan-modified biomaterials, or glycomaterials, has emerged through advances in our understanding of glycans, coupled with the development of sophisticated new techniques to identify, characterize, and synthesize them. This special section, Medical Applications of Glycomaterials, presents a collection of articles demonstrating the enormous potential of glycomaterials for lectin detection, studies of cancer cell behavior, and controlling growth factor signaling in stem cells. Lateral flow devices (LFDs) are an effective, low-cost option for point-of-care diagnosis of infection and detection of pregnancy. In typical LFD designs, a clinical sample is flowed over a paper strip that has been functionalized with a molecule that possesses binding affinity for the analyte of interest. Concurrently, a mobile “signal generating substance” phase that also possesses binding affinity for the analyte of interest is flowed over the strip. If analyte is present in the sample, it becomes sandwiched between the mobile and paper-bound stationary phases, leading to detectable accumulation of the signal generating molecule at the location of the stationary phase (i.e., a positive result). Conventional LFDs employ immobilized antibodies in the stationary and mobile phase due to the high specificity and selectivity of antibody-analyte interactions. Alternatively, recent work demonstrates that immobilized lectins can be employed for detection of glycans, or conversely immobilized glycans for detection of lectins, thereby expanding the range of analytes that can be assayed using LFDs. Developing a successful LFD requires insights into the features of the stationary and mobile phases that im","journal":"Advanced Healthcare Materials","year":2022,"id":292838,"datarank":0.0,"base_score":0.0,"endowment":0.0,"self_citation_contribution":0.0,"citation_network_contribution":0.0,"self_endowment_contribution":0.0,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":2,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":0.9547,"is_data_producer":false,"deposit_databanks":null,"is_oa":true,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":"2022-01-01","fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":418761,"name":"Gregory A. Hudalla","orcid":"0000-0003-2259-0809","position":0,"is_corresponding":true}],"reference_count":0,"raw_metadata":null,"created_at":"2026-07-19T00:30:50.076284Z","pmid":"35170235","pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}