Dear Colleagues,

Glycosaminoglycans are linear, anionic polysaccharides (GAGs) consisting of repeating disaccharides. Indeed, most GAG chains are formed from repeating disaccharide units of hexosamine and hexuronic acid. The exception is keratan sulfate, whose building blocks consist of hexosamine and galactose. Differences in the structure of the primary disaccharide unit regarding types of uronic acid and hexosamine, the number and position of the sulfate residues, the presence of N-acetyl and/or N-sulfate groups and the relative molecular mass are evident. All such differences bestow these biomolecules with impressive complexity and diversity. The fine structure of the disaccharide units defines the types of GAGs. These include chondroitin/dermatan sulfate (CS/DS), heparin/heparan sulfate (Hep/HS), and keratan sulfate (KS), as well as non-sulfated hyaluronan (HA). GAGs are ubiquitously localized throughout the extracellular matrix (ECM) and to the cell membranes of cells in all tissues. They are either conjugated to protein cores in the form of proteoglycans, e.g., CS/DS, HS, and KS or as free GAGs (HA and Hep). Through their interaction with proteins, GAGs can affect cell–ECM and cell–cell interactions, finely modulating ligand-receptor binding and, thus, chemokine and cytokine activities, as well as growth factor sequestration. Indeed, it is well established that GAGs participate in the regulation of all biological processes under homeostasis; they also participate in disease progression. Significant advances have lately been achieved in analytic, sequencing, and structural characterization of GAG oligosaccharides, as well as in GAG profiling in tissues and cells (GAGomics). Moreover, studies focused on the structure/sequence–function relationships of GAGs have resulted in critical novel insights. Furthermore, advances in the characterization of protein-GAG complexes provide invaluable tools to decipher GAG roles in the intricate tissue milieu and answer critical questions on GAG participation in the molecular basis of disease and embryonic development. The Special Issue of Biomolecules entitled "Exploring the multifaceted roles of glycosaminoglycans (GAGs)—new advances and further challenges” will feature recent findings in the analysis, sequencing, and structural characterization of GAG oligosaccharides. Such features shed light on biological processes and GAG structure/ function relationships. We invite investigators to submit reviews or regular research articles highlighting these significant advances.

Prof. Dr. Dragana Nikitovic
Dr. Serge Perez
Guest Editors

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• GAGs: Hyaluronic Acid, Heparan (Sulfate) Heparin, Heparosan
• Chondroitin
• Dermatan
• Keratan, GAGs like
• Peri and Extracellular Matrix
• Regulation & Biosynthesis of GAG
• Extraction of GAGs
• Synthesis of GAGs (chemical, metabolic engineering,...)
• Characterization of GAGs sequence
• molecular weight, degree of polymerization, 3D structures,....)
• GAGs structure/properties relationships
• GAG oligosaccharides
• Glycobiology
• GAG structure/function relationship
• Protein-GAG complexes
• GAGs in disease
• GAG-based biomaterials
• GAGs as nanocarriers