TY  - JOUR
A1  - Fischer, Sabrina
A1  - Lamping, Matthias
A1  - Gold, Maike
A1  - Röttger, Yvonne
A1  - Brödje, Dörte
A1  - Dodel, Richard
A1  - Frantz, Renate
A1  - Mraheil, Mobarak Abu
A1  - Chakraborty, Trinad
A1  - Geyer, Armin
T1  - Synthesis of a biological active β-hairpin peptide by addition of two structural motifs
JF  - Bioorganic & Medicinal Chemistry
N2  - 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 β-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 C1-C10 cyclo-CHWEGNKLVC was included in the bicyclic peptide 2. The designed β-hairpin peptide C4-C17, C8-C13 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.
KW  - Peptides
KW  - Disulfides
KW  - NMR spectroscopy
KW  - Filaggrin
Y1  - 2017
U6  - http://dx.doi.org/10.1016/j.bmc.2016.11.022
SN  - 0968-0896
VL  - 25
IS  - 2
SP  - 603
EP  - 608
ER  -