Investigation of the network of preferred interactions in an artificial coiled-coil association using the peptide array technique.
Raheleh Rezaei Araghi, Carsten C Mahrenholz, Rudolf Volkmer, Beate Koksch
Author Information
Raheleh Rezaei Araghi: Institute of Chemistry and Biochemistry, Freie Universität Berlin, Takustrasse 3, 14195 Berlin, Germany.
We screened a randomized library and identified natural peptides that bound selectively to a chimeric peptide containing α-, β- and γ-amino acids. The SPOT arrays provide a means for the systematic study of the possible interaction space accessible to the αβγ-chimera. The mutational analysis reveals the dependence of the binding affinities of α-peptides to the αβγ-chimera, on the hydrophobicity and bulkiness of the side chains at the corresponding hydrophobic interface. The stability of the resulting heteroassemblies was further confirmed in solution by CD and thermal denaturation.
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