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- W4293498849 abstract "The helix-hairpin-helix (HhH) motif in prokaryote and eukaryote DNA binding proteins is involved in non-sequence-specific DNA binding. Several studies have examined various HhH binding interactions, but the effect of stereochemistry on non-sequence-specific DNA binding by HhH peptides remains unresolved. Here, we analyzed stereochemistry-specific interactions between DNA structures and HhH motif peptides derived from NAD+-dependent DNA ligase, which is a promising target for developing new antibiotics. We synthesized l- and d-forms of single HhH motif peptides and found that both the native l-HhH-N peptide and d-HhH-N peptide bind bubble DNA and the peptides were changed to α-helical structure. Moreover, the d-HhH-N peptide showed different interaction properties against single-stranded and double-stranded DNA when compared with the l-HhH-N peptide. This study provides insights into non-sequence-specific DNA binding of d-peptides for developing d-peptide drugs. The helix-hairpin-helix (HhH) motif plays a key role in non-sequence-specific DNA binding. d-peptides are composed of d-amino acids and attractive biomolecules for medical applications. In this study, we report the interactions between l/d-HhH-N peptides and different DNA structures. The interaction of the d-HhH-N peptide with DNA is dependent on the DNA structure and shows different binding properties than l-HhH-N peptide." @default.
- W4293498849 created "2022-08-29" @default.
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- W4293498849 date "2022-10-05" @default.
- W4293498849 modified "2023-10-18" @default.
- W4293498849 title "Stereoselective Interaction of Helix-Hairpin-Helix Motif Peptides with DNA Structure" @default.
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- W4293498849 doi "https://doi.org/10.1246/cl.220340" @default.
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