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The use of Fmoc-Lys(Pac)-OH and penicillin G acylase in the preparation of novel semisynthetic insulin analogs

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JournalJOURNAL OF PEPTIDE SCIENCE
DatePublished - May 2007
Issue number5
Volume13
Number of pages8
Pages (from-to)334-341
Original languageEnglish

Abstract

In this paper, we present the detailed synthetic protocol and characterization of Fmoc-Lys(Pac)-OH, its use for the preparation of octapeptides H-Gly-Phe-Tyr-N-MePhe-Thr-Lys(Pac)-Pro-Thr-OH and H-Gly-Phe-Phe-His-Thr-Pro-Lys(Pac)-Thr-OH by solid-phase synthesis, trypsin-catalyzed condensation of these octapeptides with desoctapeptide(B23-B30) -insulin, and penicillin G acylase catalyzed cleavage of phenylacetyl (Pac) group from N'-amino group of lysine to give novel insulin analogs [TyrB25, N-MePheB26, LysB28, ProB291 -insulin and [HisB261 -insulin. These new analogs display 4 and 78% binding affinity respectively to insulin receptor in rat adipose membranes. Copyright (C) 2007 European Peptide Society and John Wiley & Sons, Ltd.

    Research areas

  • insulin analogs, semisynthesis, phenylacetyl, penicillin G acylase, PROTECTING GROUP TECHNIQUES, SOLID-PHASE SYNTHESIS, PEPTIDE-SYNTHESIS, B-CHAIN, AMINO-ACIDS, BIOLOGICAL-ACTIVITY, COUPLING REAGENTS, ENZYMATIC REMOVAL, B26-30 INSULIN, C-TERMINUS

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