Citation: Wen-Long ZHANG, Ying-Yuan HU, Ying-Li WANG, Rui LI, Jian-Li LI, Bin-Sheng YANG. Interaction of Melittin and Calf Thymus DNA[J]. Chinese Journal of Inorganic Chemistry, ;2022, 38(4): 629-636. doi: 10.11862/CJIC.2022.073 shu

Interaction of Melittin and Calf Thymus DNA

1.
College of Chinese Medicine and Food Engineering, Shanxi University of Chinese Medicine, Jinzhong, Shanxi 0300619, China
2.
Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education, Institue of Molecular Science, Shanxi University, Taiyuan 030006, China

Corresponding author: Bin-Sheng YANG, yangbs@sxu.edu.cn
Received Date: 1 November 2021
Revised Date: 20 December 2021

Figures(9)

The binding of melittin (Mel) to Calf Thymus DNA (CT-DNA) and conformation change were described by circular dichroism (CD) spectra, UV-Vis spectra, fluorescence spectra, and isothermal titration calorimetry (ITC) in 10 mmol·L^-1 HEPES buffer (pH=7.4). The results showed that Mel could form a complex with CT-DNA. The for- mation of the complex changed the conformation of Mel from random coil to α-helix as shown by CD spectra. The red edge excitation shift (REES) studies of tryptophan (Trp) residue in Mel indicated that Trp residue is located in the more hydrophobic environment in the complex with DNA, exactly as demonstrated by fluorescence lifetime and acrylamide experiments. Additionally, the double helix structure of CT-DNA changed and the CT-DNA melting tem- perature (T_m) increased from 64.3 to 66.2 ℃ once a complex was formed with Mel. Finally, the ITC experiment dem- onstrated that the binding of Mel to CT-DNA is an endothermic process. The interaction between Mel and CT-DNA was further characterized by an equilibrium association constant (K_a) of about 105 L·mol^-1. The enthalpy contribu- tion to the free energy of binding was little, and nearly three times less than the entropic term TΔS calculated from measured values of K_a and ΔH. Thus, the binding of CT -DNA to Mel is primarily driven by entropy, demonstrating electrostatic and hydrophobic interactions playing roles in the formation of the complex. The ionic strength effect and single - stranded DNA (ssDNA) quenching effect further verified that electrostatic interaction and hydrophobic interactions coexist between them and electrostatic interaction is the predominant one.
- melittin,
- CT-DNA,
- conformation,
- complex
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