ORGN 276 |
Disulfide-directed protein modification with rhodium carbenoids
| Matthew B. Francis and John M. Antos. Department of Chemistry, University of California, Berkeley, 724 Latimer Hall, Berkeley, CA 94720-1460 |
A new transition metal mediated reaction for the selective bioconjugation of disulfide bonds has been developed. The active species in this reaction is a stabilized metallocarbene (1) prepared through the reaction of vinyl diazo substrates with rhodium catalysts. This species forms ylides (2) with disulfides present on proteins and peptides, leading to stable modifications through one of two subsequent reaction pathways. In the first, an electrocyclization occurs to afford dithiane products (3). The second pathway involves capture of the ylide by an adjacent nucleophile to yield 4. Both reactions preserve the linkage between the cysteine residues and can be carried out in aqueous solution at room temperature. The development, scope, and limitations of this reaction will be presented.  |
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Proteins, Peptides, Amino Acids, and Nucleotides
1:00 PM-5:00 PM, Tuesday, March 30, 2004 Anaheim Convention Center -- 303D, Oral
Division of Organic Chemistry
The 227th ACS National Meeting, Anaheim, CA, March 28-April 1, 2004
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