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Discovery of indole-modified aptamers for highly specific recognition of protein glycoforms

Author

Listed:
  • Alex M. Yoshikawa

    (Stanford University)

  • Alexandra Rangel

    (Stanford University)

  • Trevor Feagin

    (Stanford University)

  • Elizabeth M. Chun

    (Stanford University)

  • Leighton Wan

    (Stanford University)

  • Anping Li

    (Stanford University)

  • Leonhard Moeckl

    (Stanford University)

  • Diana Wu

    (Stanford University)

  • Michael Eisenstein

    (Stanford University
    Stanford University)

  • Sharon Pitteri

    (Stanford University)

  • H. Tom Soh

    (Stanford University
    Stanford University
    Chan Zuckerberg Biohub)

Abstract

Glycosylation is one of the most abundant forms of post-translational modification, and can have a profound impact on a wide range of biological processes and diseases. Unfortunately, efforts to characterize the biological function of such modifications have been greatly hampered by the lack of affinity reagents that can differentiate protein glycoforms with robust affinity and specificity. In this work, we use a fluorescence-activated cell sorting (FACS)-based approach to generate and screen aptamers with indole-modified bases, which are capable of recognizing and differentiating between specific protein glycoforms. Using this approach, we were able to select base-modified aptamers that exhibit strong selectivity for specific glycoforms of two different proteins. These aptamers can discriminate between molecules that differ only in their glycan modifications, and can also be used to label glycoproteins on the surface of cultured cells. We believe our strategy should offer a generally-applicable approach for developing useful reagents for glycobiology research.

Suggested Citation

  • Alex M. Yoshikawa & Alexandra Rangel & Trevor Feagin & Elizabeth M. Chun & Leighton Wan & Anping Li & Leonhard Moeckl & Diana Wu & Michael Eisenstein & Sharon Pitteri & H. Tom Soh, 2021. "Discovery of indole-modified aptamers for highly specific recognition of protein glycoforms," Nature Communications, Nature, vol. 12(1), pages 1-12, December.
  • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-26933-1
    DOI: 10.1038/s41467-021-26933-1
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    Cited by:

    1. Alex M. Yoshikawa & Alexandra E. Rangel & Liwei Zheng & Leighton Wan & Linus A. Hein & Amani A. Hariri & Michael Eisenstein & H. Tom Soh, 2023. "A massively parallel screening platform for converting aptamers into molecular switches," Nature Communications, Nature, vol. 14(1), pages 1-14, December.

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