Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/133040
Citations | ||
Scopus | Web of Science® | Altmetric |
---|---|---|
?
|
?
|
Type: | Journal article |
Title: | Retro Diels-Alder fragmentation of fulvene-maleimide bioconjugates for mass spectrometric detection of biomolecules |
Author: | Stevens, K.G. McFarlane, L.O. Platts, K. O'Brien-Simpson, N. Li, W. Blencowe, A. Trim, P.J. Pukala, T.L. |
Citation: | Analytical Chemistry, 2021; 93(36):12204-12212 |
Publisher: | American Chemical Society |
Issue Date: | 2021 |
ISSN: | 0003-2700 1520-6882 |
Statement of Responsibility: | Katherine G. Stevens, Lewis O. McFarlane, Kirsten Platts, Neil O’Brien-Simpson, Wenyi Li, Anton Blencowe, Paul J. Trim, and Tara L. Pukala |
Abstract: | Diels-Alder chemistry is a well-explored avenue for the synthesis of bioactive materials; however, its potential applications have recently expanded following the development of reactions that can be performed in buffered aqueous environments at low temperatures, including fulvene-maleimide [4 + 2] cycloadditions. In this study, we synthesized two novel amine-reactive fulvene linkers to demonstrate the application of this chemistry for generating mass spectrometry-cleavable labels ("mass tags"), which can be used for the labeling and detection of proteins. Successful conjugation of these linkers to maleimide-labeled peptides was observed at low temperatures in phosphate-buffered saline, allowing the non-destructive modification of proteins with such mass tags. The labile nature of fulvene-maleimide adducts in the gas phase also makes them suitable for both matrix-assisted laser desorption/ionization (MALDI) and electrospray ionization (ESI) mass spectrometric analysis. Unlike previous examples of MALDI mass tags, we show that fulvene-maleimide cycloaddition adducts fragment predictably upon gas-phase activation without the need for bulky photocleavable groups. Further exploration of this chemistry could therefore lead to new approaches for mass spectrometry-based bioassays. |
Keywords: | Maleimides |
Rights: | © 2021 American Chemical Society |
DOI: | 10.1021/acs.analchem.1c00193 |
Grant ID: | http://purl.org/au-research/grants/arc/DP170102033 |
Published version: | http://dx.doi.org/10.1021/acs.analchem.1c00193 |
Appears in Collections: | Chemistry and Physics publications |
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.