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  Practical considerations for printing high-density glycan microarrays to study weak carbohydrate-protein interactions

Ruprecht, C., Geißner, A., Seeberger, P. H., & Pfrengle, F. (2019). Practical considerations for printing high-density glycan microarrays to study weak carbohydrate-protein interactions. Carbohydrate Research, 481, 31-35. doi:10.1016/j.carres.2019.06.006.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0003-E6CE-2 Version Permalink: http://hdl.handle.net/21.11116/0000-0006-56FD-D
Genre: Journal Article

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 Creators:
Ruprecht, Colin1, Author              
Geißner, Andreas2, Author              
Seeberger, Peter H.3, Author              
Pfrengle, Fabian1, Author              
Affiliations:
1Fabian Pfrengle, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863303              
2Chakkumal Anish, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863299              
3Peter H. Seeberger - Automated Systems, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863306              

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Free keywords: Glycan microarrays Glycan-binding proteins, Immobilization of glycans, Glycan-protein interactions
 Abstract: Interactions of carbohydrates and proteins are essential for many biological processes and glycan microarrays have emerged as powerful tools to rapidly assess these carbohydrate-protein interactions. Diverse platforms to immobilize glycans on glass slides for subsequent probing of the specificities of glycan-binding proteins (GBPs) have evolved. It has been suggested that high local glycan density on microarrays is crucial for detecting low-affinity interactions. To determine the influence of printing efficacy on GBP binding, we compared N-hydroxyl succinimide (NHS)-ester activated glass slides from three different manufacturers and evaluated two different printing buffers. Large differences in binding efficacies of Concanavalin A, peanut agglutinin, and Ricinus communis agglutinin 120 were observed. On some slides, low affinity interactions were missed altogether. Addition of polyethylenglycol (PEG) 400 to the printing buffer significantly enhanced the sensitivity of the binding assays. After monitoring printing efficacy over prolonged printing times, substantial effects resulting from progressing hydrolysis of the NHS-esters during the printing run on one type of slides were found. Printing efficiency of glycans strongly depends on the type of NHS-ester activated slides, the printing buffer, and the printing time. We provide practical advice for selecting the right printing conditions for particular applications.

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Language(s): eng - English
 Dates: 2019-06-132019
 Publication Status: Published in print
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 Identifiers: DOI: 10.1016/j.carres.2019.06.006
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Title: Carbohydrate Research
  Other : Carbohydrate Research
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 481 Sequence Number: - Start / End Page: 31 - 35 Identifier: ISSN: 0008-6215