Sep 2026· Current Opinion in Chemical Biology· Vol 94, pp. 102753 - 102753· 0 citations· 81 references
Medicine
Abstract
Proteoglycans (PGs) are intricate macromolecules decorated with linear polysulfated glycosaminoglycans (GAGs) that play critical roles in orchestrating a wide range of physiological and pathological events. Advances in the utilization of recombinant enzymes and biosynthetic pathways have expedited the production of defined and homogeneous GAGs, helping overcome traditional barriers of chemical synthesis. Furthermore, the synthesis of GAG chains has been increasingly integrated with other critical structural elements, most notably the core proteins. Robust synthetic methodologies toward well-defined GAGs and entire PG structures are critical since there is a lack of comprehensive structure-function data that addresses the PG architecture as a unified glycoconjugate. The construction of homogeneous PG is a formidable and rapidly evolving frontier in chemical biology, and the latest developments in this arena are summarized in this review.
Glycosaminoglycans (GAGs) are complex carbohydrates ubiquitously expressed on cell surfaces and within the extracellular matrix, where they regulate essential biological processes through sequence- and sulfation-dependent interactions. Major GAG classes, including heparan sulfate (HS), chondroitin sulfate (CS), dermata...
Jasper S Dumalaog, Shang-Cheng Hung· Current Opinion in Chemical...· 0 citations
Glycosaminoglycan (GAG) modifications mediate multiple biological processes, yet the GAG modification landscape remains poorly characterized, especially in invertebrates. The silkworm Bombyx mori is an important economic insect, a lepidopteran model species, and a promising bioreactor for recombinant protein production...
F. Zhu, Wen-Sheng Tao, Ting-Ting Xue et al.· International Journal of Bio...· 0 citations
The results provide a molecular-level framework for GAG-assisted maturation of procathepsin K, highlighting cooperative environmental and allosteric regulation of zymogen activation.
Damian Suchomski, P. Wesołowski, K. Bojarski· Biophysical Chemistry· 0 citations
This work employs large-scale all-atom molecular dynamics simulations to investigate the molecular origin of secondary structure in sulfated GAGs and introduces a two-parameter structural metric that objectively classifies GAG secondary structures and distinguishes heparin helices from related conformations.
Miguel Riopedre-Fernandez, Denys Biriukov, Hector Martinez-Seara· Glycobiology· 0 citations
It is concluded that, depending on the 6-O-sulfation pattern and the length of the oligosaccharide, either predominantly electrostatic interactions or a more complex interplay between electrostatic and hydrophobic interactions determines the specificity of the resulting protein-glycosaminoglycan complex.
Sergey A. Samsonov, A. Sieradzan, Avner Yayon· Glycobiology· 0 citations
We use cookies to run the site and, with your consent, for analytics and to show ads.
See our Cookie Policy.
