STICS: surface-tethered iterative carbohydrate synthesis

Pornsuriyasak, Papapida; Ranade, Sneha C.; Li, Aixiao; Parlato, Maria Cristina; Sims, Charles R.; Shulga, Olga V.; Stine, Keith J.; Demchenko, Alexei V.

doi:10.1039/b817684a

Cited by 39 publications

(46 citation statements)

References 41 publications

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“…Thioglycosides are generally much less reactive than O-imidates and hence considered less desirable for polymer-supported synthesis. With some prior success of using thioglycosides in glycosylations using polymer 46 and nanoporous supports 43 we investigated S-benzoxazolyl (SBox) donor 4 59 and S-phenyl glycosyl donor 5 60 in the HPLC-automated reactions. Glycosylation of SBox donor 4 with resin-bound acceptor 3 was performed in the presence of AgOTf.…”

Section: Resultsmentioning

confidence: 99%

HPLC-Assisted Automated Oligosaccharide Synthesis: Implementation of the Autosampler as a Mode of the Reagent Delivery

et al. 2016

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The development of a useful methodology for simple, scalable, and transformative automation of oligosaccharide synthesis that easily interfaces with existing methods is reported. The automated synthesis can now be performed using accessible equipment where the reactants and reagents are delivered by the pump or the autosampler and the reactions can be monitored by the UV detector. The HPLC-based platform for automation is easy to setup and adapt to different systems and targets.

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Section: Resultsmentioning

confidence: 99%

HPLC-Assisted Automated Oligosaccharide Synthesis: Implementation of the Autosampler as a Mode of the Reagent Delivery

et al. 2016

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“…22,33,34,58,106,107 The stability of np-Au monoliths to solution flow through the pores makes the material potentially attractive for applications in separations of biomacromolecules. To further examine the potential of np-Au as a platform for use in glycoscience, we applied TGA to assess the binding of Con A, a lectin with high specificity for α-D-mannosyl residues, to np-Au monoliths modified with both pure and mixed SAMs of αMan-C 8 -SH.…”

Section: Resultsmentioning

confidence: 99%

Lectin–carbohydrate interactions on nanoporous gold monoliths

et al. 2013

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Monoliths of nanoporous gold (np-Au) were modified with self-assembled monolayers of octadecanethiol (C18-SH), 8-mercaptooctyl α-D-mannopyranoside (αMan-C8-SH), and 8-mercapto-3,6-dioxaoctanol (HO-PEG2-SH), and the loading was assessed using thermogravimetric analysis (TGA). Modification with mixed SAMs containing αMan-C8-SH (at a 0.20 mole fraction in the SAM forming solution) with either octanethiol or HO-PEG2-SH was also investigated. The np-Au monoliths modified with αMan-C8-SH bind the lectin Concanavalin A (Con A), and the additional mass due to bound protein was assessed using TGA analysis. A comparison of TGA traces measured before and after exposure of HO-PEG2-SH modified np-Au to Con A showed that the non-specific binding of Con A was minimal. In contrast, np-Au modified with octanethiol showed a significant mass loss due to non-specifically adsorbed Con A. A significant mass loss was also attributed to binding of Con A to bare np-Au monoliths. TGA revealed a mass loss due to the binding of Con A to np-Au monoliths modified with pure αMan-C8-SH. The use of mass losses determined by TGA to compare the binding of Con A to np-Au monoliths modified by mixed SAMs of αMan-C8-SH and either octanethiol or HO-PEG2-SH revealed that binding to mixed SAM modified surfaces is specific for the mixed SAMs with HO-PEG2-SH but shows a significant contribution from non-specific adsorption for the mixed SAMs with octanethiol. Minimal adsorption of immunoglobulin G (IgG) and peanut agglutinin (PNA) towards the mannoside modified np-Au monoliths was demonstrated. A greater mass loss was found for Con A bound onto the monolith than for either IgG or PNA, signifying that the mannose presenting SAMs in np-Au retain selectivity for Con A. TGA data also provide evidence that Con A bound to the αMan-C8-SH modified np-Au can be eluted by flowing a solution of methyl α-D-mannopyranoside through the structure. The presence of Con A proteins on the modified np-Au surface was also confirmed using atomic force microscopy (AFM). The results highlight the potential for application of carbohydrate modified np-Au monoliths to glycoscience and glycotechnology and demonstrate that they can be used for capture and release of carbohydrate binding proteins in significant quantities.

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“…Although oligosaccharide synthesis on solid, soluble polymer, and tag supports has been dramatically developed as described, a high level of technical expertise is still required for the oligosaccharide synthesis. As the direct construction and assay techniques of the oligosaccharides library on the array, 110 as well as the utilization of the new surface platform for the iterative glycan synthesis, 111 have rapidly been emerging, further improvements in the oligosaccharide synthesis on the solid supports is expected to establish the general and efficient methods, which will speed up the elucidation of the biological functions of oligosaccharides as well as clinical applications of oligosaccharide-based drugs. …”

Section: Discussionmentioning

confidence: 99%