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Updated: May 12, 2026

CD Spectroscopy to Study DNA-Protein Interactions
Published on: February 10, 2022
Interaction mechanism of Trp-Arg dipeptide with calf thymus DNA
Jing Lin1, Canzhu Gao, Rutao Liu
1Shandong Key Laboratory of Water Pollution Control and Resource Reuse, School of Environmental Science and Engineering, China-America CRC for Environment & Health, Shandong University, Shandong Province, Jinan, People's Republic of China.
Abstract:
The interaction between Trp-Arg dipetide (WR) and calf thymus DNA (ctDNA) in pH 7.4 Tris-HCl buffer was investigated by multi-spectroscopic techniques and molecular modeling. The fluorescence spectroscopy and UV absorption spectroscopy indicated that WR interacted with ctDNA in a minor groove binding mode and the binding constant was 4.1 × 10(3). The ionic strength effect and single-stranded DNA (ssDNA) quenching effect further verified the minor groove binding mode. Circular dichroism spectroscopy (CD) was employed to measure the conformation change of ctDNA in the presence of WR. The molecular modeling results illustrated that electrostatic interaction and groove binding coexisted between them and the hydrogen bond and Van der Waals were main acting forces. All the above methods can be widely used to investigate the interaction of peptide with nucleic acids, which contributes to design the structure of new and efficient drugs.
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