Iodination of Proteins by IPy2BF4, a New Tool in Protein Chemistry†
journal contributionposted on 16.05.2006 by Gemma Espuña, David Andreu, José Barluenga, Xavier Pérez, Antoni Planas, Gemma Arsequell, Gregorio Valencia
Any type of content formally published in an academic journal, usually following a peer-review process.
Iodination is a very useful method for protein characterization and labeling. However, derivatization chemistries used in most conventional iodination procedures may cause substantial alterations in protein structure and function. The IPy2BF4 reagent [bis(pyridine)iodonium (I) tetrafluoroborate] has been shown to be an effective iodinating reagent for peptides. Herein we report the first application of IPy2BF4 in protein iodination in an aqueous medium using three representative substrates: insulin, lysozyme, and the enzyme 1,3-1,4-β-d-4-glucanohydrolase. Our results show that IPy2BF4 has clear advantages over existing methods in that the reaction is quantitative, fast, and selective for the most accessible Tyr residues of a protein, and it preserves the functional integrity of the protein when moderate Tyr labeling levels are pursued.