Rapid and Modular Assembly of Click Substrates To Assay Enzyme Activity in the Newborn Screening of Lysosomal Storage Disorders Article Swipe
Philipp Skrinjar
,
Markus Schwarz
,
Stefan Lexmüller
,
Thomas P. Mechtler
,
Maximilian Zeyda
,
Susanne Greber‐Platzer
,
Joe Trometer
,
David C. Kasper
,
Hannes Mikula
·
YOU?
·
· 2018
· Open Access
·
· DOI: https://doi.org/10.1021/acscentsci.8b00668
YOU?
·
· 2018
· Open Access
·
· DOI: https://doi.org/10.1021/acscentsci.8b00668
Synthetic substrates play a pivotal role in the development of enzyme assays for medical diagnostics. However, the preparation of these chemical tools often requires multistep synthetic procedures complicating structural optimization and limiting versatility. In particular, substrates for enzyme assays based on tandem mass spectrometry need to be designed and optimized to fulfill the requirements to finally enable the development of robust diagnostic assays. In addition, isotope-labeled standards need to be prepared to facilitate accurate quantification of enzyme assay products. Here we report the development of a building block strategy for rapid and modular assembly of enzyme substrates using click chemistry as a key step. These click substrates are made up of a sugar moiety as enzyme responsive unit, a linker that can easily be isotope-labeled for the synthesis of internal standards, and a modifier compound that can readily be exchanged for structural optimization and analytical/diagnostic tuning. Moreover, the building block assembly eliminates the need for extensive optimization of different glycosylation reactions as it enables the divergent synthesis of substrates using a clickable enzyme responsive unit. The outlined strategy has been applied to obtain a series of synthetic α-l-iduronates and sulfated β-d-galactosides as substrates for assaying α-l-iduronidase and N-acetylgalactosamine-6-sulfate sulfatase, enzymes related to the lysosomal storage disorders mucopolysaccharidosis type I and type IVa, respectively. Selected click substrates were finally shown to be suitable to assay enzyme activities in dried blood spot samples from affected patients and random newborns.
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- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1021/acscentsci.8b00668
- https://pubs.acs.org/doi/pdf/10.1021/acscentsci.8b00668
- OA Status
- diamond
- Cited By
- 13
- References
- 60
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W2903850424
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Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W2903850424Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.1021/acscentsci.8b00668Digital Object Identifier
- Title
-
Rapid and Modular Assembly of Click Substrates To Assay Enzyme Activity in the Newborn Screening of Lysosomal Storage DisordersWork title
- Type
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articleOpenAlex work type
- Language
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enPrimary language
- Publication year
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2018Year of publication
- Publication date
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2018-12-06Full publication date if available
- Authors
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Philipp Skrinjar, Markus Schwarz, Stefan Lexmüller, Thomas P. Mechtler, Maximilian Zeyda, Susanne Greber‐Platzer, Joe Trometer, David C. Kasper, Hannes MikulaList of authors in order
- Landing page
-
https://doi.org/10.1021/acscentsci.8b00668Publisher landing page
- PDF URL
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https://pubs.acs.org/doi/pdf/10.1021/acscentsci.8b00668Direct link to full text PDF
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YesWhether a free full text is available
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diamondOpen access status per OpenAlex
- OA URL
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https://pubs.acs.org/doi/pdf/10.1021/acscentsci.8b00668Direct OA link when available
- Concepts
-
Click chemistry, Enzyme, Combinatorial chemistry, Chemistry, Linker, Biochemistry, Computer science, Operating systemTop concepts (fields/topics) attached by OpenAlex
- Cited by
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13Total citation count in OpenAlex
- Citations by year (recent)
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2025: 1, 2024: 2, 2023: 3, 2022: 3, 2021: 2Per-year citation counts (last 5 years)
- References (count)
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60Number of works referenced by this work
- Related works (count)
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10Other works algorithmically related by OpenAlex
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