Specific recognition of single-stranded nucleic acids. Interaction of tryptophan-containing peptides with native, denatured, and ultraviolet-irradiated DNA.
The binding of the tripeptide Lys-Trp-Lys to native, denatured, and ultraviolet-irradiated DNAs has been investigated by fluorescence spectroscopy. Two types of complexes are formed which both involve electrostatic interactions. Only one of them involves a stacking of the tryptophyl ring with nucleic acid bases. Quantitative analysis of fluorescence data shows that this stacking interaction is strongly favored in denatured as compared to native DNA. In ultraviolet-irradiated DNA, the peptide Lys-Trp-Lys binds selectively to unpaired regions around thymine dimers. Due to the stacking interaction of the aromatic amino acid with nucleic acid bases, this simple tripeptide is therefore able to discriminate between single-stranded and double-stranded regions in a nucleic acid.
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002942:Circular Dichroism; D004277:DNA, Single-Stranded / Q000528:radiation effects; D008239:Lysine; D009690:Nucleic Acid Conformation; D009691:Nucleic Acid Denaturation; D009842:Oligopeptides; D011485:Protein Binding; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D013950:Thymus Gland; D014364:Tryptophan; D014466:Ultraviolet Rays
D004277:DNA, Single-Stranded; D009842:Oligopeptides; D014364:Tryptophan; D008239:Lysine