AI Article Synopsis
- Researchers explored a method to synthesize glycosaminoglycan chains and connect them to peptides using proteoglycans.
- In this process, the enzyme hyaluronidase facilitates a reaction that releases and transfers sugar units to create customized glycosaminoglycan chains.
- This technique offers the potential to produce consistent and uniform proteoglycans or their analogues for various applications.
Article Abstract
A method for the synthesis of carbohydrate chains (glycosaminoglycans) and their coupling to peptides was investigated using proteoglycans. Glycosidases generally catalyze a hydrolytic reaction, but can also mediate the reverse reaction, which in this case is a transglycosylation. In the transglycosylation reaction of bovine testicular hyaluronidase, which is an endoglycosidase, glycosaminoglycans (hyaluronan and chondroitin sulfates) release disaccharide (uronic acid-N-acetylhexosamine) moieties from non-reducing terminal sites, and then the liberated disaccharides are transferred immediately to the non-reducing termini of other glycosaminoglycan chains. Using such continuous reactions, it is possible to synthesize glycosaminoglycan chains according to a specific design. It then becomes possible to transfer glycosaminoglycan chains synthesized on a peptide to other peptides using the transglycosylation reaction of endo-β-xylosidase acting on the linkage region between a peptide and glycosaminoglycan chains of proteoglycans. We believe this approach will open a new field for the synthesis of homogeneous proteoglycans or their corresponding analogues.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3422686 | PMC |
| http://dx.doi.org/10.2183/pjab.88.327 | DOI Listing |
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