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Beilstein J Org Chem. 2012;8:640-9. doi: 10.3762/bjoc.8.71. Epub 2012 Apr 25.

Investigation of the network of preferred interactions in an artificial coiled-coil association using the peptide array technique.

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1
Institute of Chemistry and Biochemistry, Freie Universität Berlin, Takustrasse 3, 14195 Berlin, Germany.

Abstract

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.

KEYWORDS:

SPOT technique; coiled coil; foldamer; screening libraries; β- and γ-amino acids

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