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Identification of small peptides mimicking the R2 C ‐terminus of Mycobacterium tuberculosis ribonucleotide reductase
Author(s) -
Ericsson Daniel J.,
Nurbo Johanna,
Muthas Daniel,
Hertzberg Kalle,
Lindeberg Gunnar,
Karlén Anders,
Unge Torsten
Publication year - 2010
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1214
Subject(s) - ribonucleotide reductase , mycobacterium tuberculosis , biochemistry , chemistry , binding site , acetylation , peptide sequence , protein subunit , peptide , amino acid , mycobacterium , biology , stereochemistry , tuberculosis , bacteria , genetics , gene , medicine , pathology
Ribonucleotide reductase (RNR) is a viable target for new drugs against the causative agent of tuberculosis, Mycobacterium tuberculosis . Previous work has shown that an N ‐acetylated heptapeptide based on the C ‐terminal sequence of the smaller RNR subunit can disrupt the formation of the holoenzyme sufficiently to inhibit its function. Here the synthesis and binding affinity, evaluated by competitive fluorescence polarization, of several truncated and N ‐protected peptides are described. The protected single‐amino acid Fmoc‐Trp shows binding affinity comparable to the N ‐acetylated heptapeptide, making it an attractive candidate for further development of non‐peptidic RNR inhibitors. Copyright © 2010 European Peptide Society and John Wiley & Sons, Ltd.