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Photochemical Depolymerisation of Dermatan Sulfate and Analysis of the Generated Oligosaccharides

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Photochemical Depolymerisation of Dermatan Sulfate and Analysis of the Generated Oligosaccharides Edinburgh Research Explorer Photochemical depolymerisation of dermatan sulfate and analysis of the generated oligosaccharides Citation for published version: Panagos, CG, August, DP, Jesson, C & Uhrin, D 2016, 'Photochemical depolymerisation of dermatan sulfate and analysis of the generated oligosaccharides', Carbohydrate polymers, vol. 140, pp. 13-19. https://doi.org/10.1016/j.carbpol.2015.11.078 Digital Object Identifier (DOI): 10.1016/j.carbpol.2015.11.078 Link: Link to publication record in Edinburgh Research Explorer Document Version: Peer reviewed version Published In: Carbohydrate polymers General rights Copyright for the publications made accessible via the Edinburgh Research Explorer is retained by the author(s) and / or other copyright owners and it is a condition of accessing these publications that users recognise and abide by the legal requirements associated with these rights. Take down policy The University of Edinburgh has made every reasonable effort to ensure that Edinburgh Research Explorer content complies with UK legislation. If you believe that the public display of this file breaches copyright please contact [email protected] providing details, and we will remove access to the work immediately and investigate your claim. Download date: 25. Sep. 2021 1 1 Photochemical depolymerisation of dermatan sulfate and analysis of the generated 2 oligosaccharides. 3 Charalampos G. Panagos, a,b David P. August,a Christine Jesson,b Dušan Uhrín a,* a 4 EastChem School of Chemistry, The University of Edinburgh, King´s Buildings, David Brewster Road , 5 Edinburgh EH9 3FJ, United Kingdom. 6 b GlycoMar Ltd, European Centre for Marine Biotechnology, Oban, Scotland, PA37 1QA, United Kingdom. 7 8 *To whom correspondence should be addressed: EaStCHEM School of Chemistry, Joseph Black Bldg., 9 The King’s Buildings, University of Edinburgh, Edinburgh, EH9 3FJ, United Kingdom. Tel.: 44-131-650- 10 4742; Fax: 44-131-650-7155; E-mail: [email protected]. 11 12 Abstract 13 Radical depolymerisation is the method of choice for the depolymerisation of glycosaminoglycans 14 (GAGs), especially when enzymatic depolymerisation cannot be performed due to the lack of suitable 15 enzymes. The established Fenton type free radical depolymerisation generates radicals from a solution 2+ 2+ 16 of H2O2 in the presence of Cu or Fe . When applied to dermatan sulfate (DS), the Fenton type 17 depolymerisation of DS (Panagos, Thomson, Bavington & Uhrin, 2012)produced exclusively 18 oligosaccharides with reducing end GalNAc , which was partially oxidized to acetylgalactosaminic acid. 19 We report here the results of the TiO2 catalyzed photochemical depolymerisation of DS. NMR analysis of 20 these DS oligosaccharides revealed the presence of reducing end IdoA, observed for the first time. The 21 reducing end acetylgalactosaminic acid was also detected. The photochemical depolymerisation method 22 thus enables preparation of new types of GAG oligosaccharides suitable for further biochemical and 23 biological investigation. 24 25 Highlights 26 Free radical photochemical depolymerisation generates GAG oligosaccharides. 27 The structures of DS oligosaccharides were studied by NMR. 28 Oligosaccharides with uronic acid as the reducing end monosaccharides were found. 29 Acetylgalactosaminic reducing end monosaccharides were also generated. 30 No desulfation of the generated oligosaccharides was found. 31 32 Keywords 33 NMR; glycosaminoglycans; dermatan sulfate; photochemical depolymerisation. 34 35 2 36 Chemical compounds studied in this article 37 Phosphate-buffered saline (PubChem CID: 24978514); Titanium dioxide (PubChem CID: 26042), 38 Ethylenediaminetetraacetic acid (PubChem CID: 6049), Trimethylsilyl propionate (PubChem CID: 39 519321), Dermatan sulfate (Pubchem CID:32756). 40 Abbreviations 41 GAGs, glycosaminoglycans; LMWH, low molecular weight heparin; DS, dermatan sulfate; GalNAc, N- 42 acetylgalactosamine; IdoA, iduronic Acid; HSQC, Heteronuclear single quantum coherence; TOCSY, Total 43 correlation spectroscopy; HMBC, Heteronuclear multiple bond coherence; 44 45 1. Introduction 46 47 Glycosaminoglycans (GAGs) are a biologically important class of carbohydrates usually found on cell 48 surfaces in the form of proteoglycans (Dietrich, Sampaio, Montesdeoca & Nader, 1980; Mathews, 1975; 49 Medeiros, Mendes, Castro, Baú, Nader & Dietrich, 2000). They are essential for a variety of cell-cell 50 signaling events, such as cell growth and cell adhesion (Singer, 1992). As long unbranched 51 polysaccharides, GAGs also participate in the construction of connective tissues (Comper & Laurent, 52 1978; Mathews, 1975), such as cartilage. The ability of GAGs to be involved in such a variety of 53 biochemical processes is underpinned by their inherent structural heterogeneity. 54 GAGs are built from repeating disaccharide units, which typically consist of an uronic acid (iduronic 55 acid or glucuronic acid) and a hexosamine (galactosamine or glucosamine). Furthermore, these 56 disaccharide units can be sulfated at different sites and the position and type of the glycosidic linkage 57 also varies between GAG types. These attributes lead to structural variety within the GAG family. 58 Although not random, the epimerization and sulfation events are not regular, creating large 59 heterogeneity within a single GAG type. For example, during the processing of heparan, the precursor of 60 heparan sulfate (HS), various enzymes including N-deacetylases/N-sulfotransferases, as well as 6-O- and 61 3-O sulfotransferases and C-5 epimerases, modify its structure, though these modifications are neither 62 random or complete (Vreys & David, 2007). The resulting macroscopic organization of HS shows a typical 63 ‘block structure’ containing extensive structural heterogeneity (Gallagher, 2006). 64 In order to study the biology and pharmacology of these heterogeneous polysaccharides it is 65 necessary to identify specific structures within their chains, which are responsible for their distinct 66 biological properties (Toida, Sato, Sakamoto, Sakai, Hosoyama & Linhardt, 2009). For example, the study 67 of heparin oligosaccharides revealed the existence of a specific pentasaccharide sequence responsible 68 for the binding of heparin to antithrombin (Munoz & Linhardt, 2004). GAG oligosaccharides are also 69 important in their own right, e.g. low molecular weight heparin (LMWH) (Choay, Lormeau, Petitou, Sinaÿ 70 & Fareed, 1981), has almost completely replaced unfractionated heparin as a pharmaceutical (Hileman, 71 Smith, Toida & Linhardt, 1997). Low molecular weight dermatan sulfates (DS) also show increased 72 bioavailability without the loss of bioactivity (Dol et al., 1990; Legnani et al., 1994). 3 73 Smaller GAG oligosaccharides can lead to a reduction in the adverse effects sometimes associated 74 with full-length polysaccharides. For example, LMWH decreases the occurrence of heparin induced 75 thrombocytopenia due to less efficient interaction with platelet factor 4 (Gray, Mulloy & Barrowcliffel, 76 2008). LMWH also reduces the risk of osteoporosis, another side effect of heparin (Matzsch, Bergqvist, 77 Hedner, Nilsson & Ostergaard, 1990; Monreal, Vinas, Monreal, Lavin, Lafoz & Angles, 1990). Another 78 example is the depolymerisation of fucosylated chondroitin sulfate, fCS, from sea cucumber (Panagos et 79 al., 2014; Suzuki, Kitazato, Takamatsu & Saito, 1991; Wu, Xua, Zhao, Kang & Ding, 2010; Wu et al., 2013; 80 Yang, Wang, Jiang, Lv, Zhang & Lv, 2015), which is critical for antithrombotic applications, due to an 81 undesired platelet aggregation associated with long polysaccharide chains (Wu, Xu, Zhao, Kang & Ding, 82 2010b). 83 Depolymerisation of GAGs and the production of fully characterised oligosaccharides is therefore 84 an essential process in evaluation of the biological potential of these molecules. A variety of different 85 depolymerisation methods, characterized by specific advantages and limitations, have therefore been 86 developed to date. The most widely used is enzymatic depolymerisation, although this method also has 87 its limitations. For example, highly sulfated GAGs, which are typical for marine species, are resistant to 88 enzymatic depolymerisation (Vieira, Mulloy & Mourao, 1991). Moreover, oligosaccharides generated by 89 heparanases and chondroitinases contain an unsaturated uronate residue as the non-reducing end 90 monosaccharide and a hexosamine as the reducing end monosaccharide (Pervin, Gallo, Jandik, Han & 91 Linhardt, 1995). Finally, depolymerisation enzymes can be very expensive, e.g. one mg of chondroitinase 92 ABC lyase, which can deliver between 50 to 250 units, can cost much more than £ 1000. 93 Other depolymerisation methods include acid hydrolysis, solvolysis and ultrasonication. Acid 94 hydrolysis is a chemically based approach which involves both the depolymerisation and the desulfation 95 of the polysaccharide (Mourao et al., 1996) and for that reason it is not widely used on sulfated GAGs. 96 Solvolytic depolymerisation has also been shown to be effective on GAGs but it also involves 97 desulfonation of the polysaccharide chains and is also known to structurally modify the oligosaccharide 98 products (Toida, Sato, Sakamoto, Sakai, Hosoyama & Linhardt, 2009). Ultrasonic depolymerisation is 99 unique among the depolymerisation methods, as it is a mechanical method, which has been employed 100 for the depolymerisation of hyaluronic acid (Miyazaki, Yomota & Okada, 2001). Although this technique 101 generates lower molecular weight
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