Synthesis of Biotin-containing Peptides Representing the Biotin Binding Site of E. coli Acetyl–CoA Carboxylase

Abstract
Two biotin-containing peptides, Ac–Met–Bct–Met–Met–OMe (1) and Boc–Met–Bct–Met–Met, that correspond to the local sequence of biotin carboxyl carrier protein subunit of E. coli acetyl–CoA carboxylase have been synthesized. The precursor tetrapeptide Boc–Met–Lys(Cbz)–Met–Met–OMe was prepared first by the stepwise elongation method and biotin was incorporated subsequently by the active ester method. Another biotin-containing peptide, HCO–Met–Bct–Met–Met–OMe, has also been prepared. Magnesium ion binding to peptide 1 in acetonitrile has been studied by means of 13C NMR spectroscopy. The metal interacts principally with the amide carbonyls rather than sulfide moieties, as deduced from a significant downfield shift of the former carbon signals in 13C NMR.

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