Rapid flow-based synthesis of post-translationally modified peptides and proteins: a case study on MYC's transactivation domain
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Abstract
Automated flow peptide synthesis (AFPS) gives access to peptides and proteins with post-translational modifications (PTMs) and enables investigation of PTM-mediated regulation, and was used to study the PTM-dependence of the MYC:Bin1 interaction.
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- Authors
- Williams, E. T., Schiefelbein, K., Schuster, M., Ahmed, I. M. M., De Vries, M., Beveridge, R., Zerbe, O., & Hartrampf, N.
- Affiliations
- University of Zurich (CH)
- University of Strathclyde (GB)
- Department for Pure and Applied Chemistry, University of Strathclyde, 295 Cathedral St, Glasgow G1 1XL, UK
- Corresponding author
- Hartrampf, Nina
- ORCID
- Venue
- Chemical Science
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2024
- Volume
- 15
- Issue
- 23
- Pages
- 8756-8765
- ISSN
- 2041-6520 (ISSN-L)
- 2041-6539
- PMC
- PMC11168107
- OpenAlex
- W4396698955
- Cited by
- 13
- References
- 55
- Citations by year
- 2026: 6 · 2025: 5 · 2024: 2
- FWCI
- 1.77
- Type
- journal article
- Language
- en
- Open access
- diamond
- doi.org
- Locations
- Chemical Science (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Zurich Open Repository and Archive (University of Zurich) (submittedVersion, cc-by)
- Funders
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (project grant no. 200021_200865 (N. H.))
- University of Strathclyde (Chancellor's Fellowship (R. B.))
- Universität Zürich (UZH PostDoc grant (E. T. W.))
- Dr. Helmut Legerlotz-Stiftung ((N. H.))
- UK Research and Innovation (MR/T020970/1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Physical Sciences › Chemistry › Organic Chemistry › Click Chemistry and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Keywords
- post-translational modification, peptide synthesis, BIN1, protein-protein interaction, phosphorylation, glycosylation, methylation, sulfation, acetylation, heteronuclear NMR, native mass spectrometry, protein analogues
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