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Allyl Sulfides Are Privileged Substrates in Aqueous Cross-Metathesis: Application to Site-Selective Protein Modification
Abstract
Allyl sulfides undergo efficient cross-metathesis in aqueous media with Hoveyda-Grubbs second generation catalyst 1. The high reactivity of allyl sulfides in cross-metathesis was exploited in the first examples of cross-metathesis on a protein surface. S-Allylcysteine was incorporated chemically into the protein, providing the requisite allyl sulfide handle. Preliminary efforts to genetically incorporate S-allylcysteine into proteins are also reported.
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Cited by
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Chemical Modification of Proteins at Cysteine: Opportunities in Chemistry and Biology
Chalker, J. M., Bernardes, G. J. L., Lin, Y. A., & Davis, B. G. (2009) · Chemistry – An Asian Journal · doi:10.1002/asia.200800427 · Cited by 649
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Methods for converting cysteine to dehydroalanine on peptides and proteins
Chalker, J. M., Gunnoo, S. B., Boutureira, O., Gerstberger, S. C., Fernández-González, M., Bernardes, G. J. L., Griffin, L., Hailu, H., Schofield, C. J., & Davis, B. G. (2011) · Chemical Science · doi:10.1039/c1sc00185j · Cited by 367
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Metadata
- Authors
- Lin, Y. A., Chalker, J. M., Floyd, N., Bernardes, G. J. L., & Davis, B. G.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2008-07-01
- Volume
- 130
- Issue
- 30
- Pages
- 9642-9643
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2118292315
- Cited by
- 330
- References
- 0
- FWCI
- 13.21
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Allyl Sulfides Are Privileged Substrates in Aqueous Cross-Metathesis: Application to Site-Selective Protein Modification. https://app.cochat.ai/papers/10.1021/ja8026168
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- Lin, Y. A., Chalker, J. M., Floyd, N., Bernardes, G. J. L., & Davis, B. G. (2008). Allyl Sulfides Are Privileged Substrates in Aqueous Cross-Metathesis: Application to Site-Selective Protein Modification. Journal of the American Chemical Society. https://doi.org/10.1021/ja8026168
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