ORGN 61 |
| The broad utility of protein bioconjugates has created a need for new and diverse strategies for site-selective protein modification. In particular, chemical reactions that target alternative amino acid side chains or unnatural functional groups are emerging as a valuable complement to more commonly used lysine and cysteine based strategies. Recently we have reported several new reactions that can modify proteins under mild aqueous buffer conditions, including a three-component Mannich-type coupling reaction for tyrosine residues, tryptophan modification using rhodium carbenoids, the attachment of lipids to tyrosine residues using pi-allylpalladium complexes, and a simple biomimetic strategy for the functionalization of the N-termini. The scope and applications of these new strategies will be discussed, as well as the reaction design concepts that are emerging from these studies. |
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Young Investigators Symposium
1:00 PM-5:00 PM, Sunday, 10 September 2006 Moscone Center -- Room 135, Oral
Division of Organic Chemistry |