Journal article

Publication year: 2017

Pages: 603-608

Journal: Bioorganic & Medicinal Chemistry

Volume number: 25

Issue number: 2

ISSN: 0968-0896

eISSN: 1464-3391

DOI Link: https://doi.org/10.1016/j.bmc.2016.11.022

Publisher: Elsevier

Abstract: 
The idea of privileged scaffolds - that there seem to be more bioactive compounds found around some structures than others - is well established for small drug molecules, but has little significance for standalone peptide secondary structures whose adaptable shapes escape the definition of a 3D motif in the absence of a protein scaffold. Here, we joined two independent biological functions in a single highly restricted peptide to support the hypothesis that the beta-hairpin shape is the common basis of two otherwise unrelated biological recognition processes. To achieve this, the hydrophobic cluster HWX4LV from the decapeptide cyclic hairpin model peptide C-1-C-10 cyclo-CHWEGNKLVC was included in the bicyclic peptide 2. The designed beta-hairpin peptide C-4-C-17, C-8-C-13 bicyclo-KHQCHWECTZGRCRLVCGRSGS (2, Z = citrulline), serves, on the one hand, as a specific epitope for rheumatoid autoantibodies and, on the other hand, shows a not negligible antibiotic effect against the bacterial strain E. coli AS19. (C) 2016 Elsevier Ltd. All rights reserved.

Harvard Citation style: Fischer, S., Lamping, M., Gold, M., Roettger, Y., Broedje, D., Dodel, R., et al. (2017) Synthesis of a biological active β-hairpin peptide by addition of two structural motifs, Bioorganic & Medicinal Chemistry, 25(2), pp. 603-608. https://doi.org/10.1016/j.bmc.2016.11.022

APA Citation style: Fischer, S., Lamping, M., Gold, M., Roettger, Y., Broedje, D., Dodel, R., Frantz, R., Abu Mraheil, M., Chakraborty, T., & Geyer, A. (2017). Synthesis of a biological active β-hairpin peptide by addition of two structural motifs. Bioorganic & Medicinal Chemistry. 25(2), 603-608. https://doi.org/10.1016/j.bmc.2016.11.022