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Heterochiral Jun and Fos bZIP peptides form a coiled‐coil heterodimer that is competent for DNA binding

Coiled coils, consisting of at least two α‐helices, have important roles in the regulation of transcription, cell differentiation, and cell growth. Peptides composed of d‐amino acids (d‐peptides) have received great attention for their potential in biomedical applications, because they give large diversity for the design of peptidyl drug and are more resistant to proteolytic digestion than l‐peptides. However, the interactions between l‐peptides/l‐protein and d‐peptides in the formation of complex are poorly understood. In this study, stereoisomer‐specific peptides were constructed corresponding to regions of the basic‐leucine‐zipper domains of Jun and Fos proteins. basic‐leucine‐zipper domains consist of an N‐terminal basic domain, which is responsible for DNA binding, and a C‐terminal domain that enables homodimerization or heterodimerization via formation of a coiled‐coil. By combining peptides with different stereochemistries, the d‐l heterochiral Jun‐Fos heterodimer formation induced DNA binding by the basic domains of Jun‐Fos. Our study provides new insight into the interaction between l‐peptide and d‐peptide enantiomers for developing d‐peptide materials and drugs. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd.