• Spectroscopy and Spectral Analysis
  • Vol. 42, Issue 7, 2107 (2022)
Xiao-qing XU*, Qian ZHOU1;, Jian-hua SUN1;, Li-xia SUN1;, Xue-zhen FENG1; 2;, Yong-fang XU1;, Zhang-fa TONG1;, and Dan-kui LIAO1; *;
Author Affiliations
  • 1. Guangxi Key Laboratory of Petrochemical Resource Processing and Process Intensification Technology, School of Chemistry and Chemical Engineering, Guangxi University, Nanning 530000, China
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    DOI: 10.3964/j.issn.1000-0593(2022)07-2107-06 Cite this Article
    Xiao-qing XU, Qian ZHOU, Jian-hua SUN, Li-xia SUN, Xue-zhen FENG, Yong-fang XU, Zhang-fa TONG, Dan-kui LIAO. Study on the Inhibition Mechanism of Angiotensin Conversion Enzyme Inhibitor Peptide Leu-Lys-Pro[J]. Spectroscopy and Spectral Analysis, 2022, 42(7): 2107 Copy Citation Text show less
    Fluorescence emission spectra of ACE with LKP at different temperatures(a)—(c): 288, 293, 298 K, c(ACE)= 1.0×10-6 mol·L-1
    Fig. 1. Fluorescence emission spectra of ACE with LKP at different temperatures
    (a)—(c): 288, 293, 298 K, c(ACE)= 1.0×10-6 mol·L-1
    The Stern-Volmer plots of ACE with LKP
    Fig. 2. The Stern-Volmer plots of ACE with LKP
    UV absorption spectra of ACE with LKP at different temperatures(a)—(c): 288, 293, 298 K,c(ACE)=1.0×10-6 mol·L-1,c(LKP)(0—4): 0, 0.28, 1.4, 2.8, 4.2×10-3 mol·L-1
    Fig. 3. UV absorption spectra of ACE with LKP at different temperatures
    (a)—(c): 288, 293, 298 K,c(ACE)=1.0×10-6 mol·L-1,c(LKP)(0—4): 0, 0.28, 1.4, 2.8, 4.2×10-3 mol·L-1
    CD spectra of ACE with LKP298 K, c(ACE)= 1.0×10-6 mol·L-1
    Fig. 4. CD spectra of ACE with LKP
    298 K, c(ACE)= 1.0×10-6 mol·L-1
    The heat flow of binding LKP to ACE(a)—(c): 288, 293, 298 K, c(ACE)=0.4 μmol·L-1, c(LKP)=2.8 mmol·L-1
    Fig. 5. The heat flow of binding LKP to ACE
    (a)—(c): 288, 293, 298 K, c(ACE)=0.4 μmol·L-1, c(LKP)=2.8 mmol·L-1
    The docking simulation of LKP binding to ACE(a): The docking simulation of LKP binding to ACE;(b): The interaction between LKP and the residues of ACE is shown
    Fig. 6. The docking simulation of LKP binding to ACE
    (a): The docking simulation of LKP binding to ACE;(b): The interaction between LKP and the residues of ACE is shown
    T/
    K
    KSV/
    (104 L·mol-1)
    Kq/
    (1012 L·s-1·mol-1)
    R2
    2884.64.61
    2932.12.10.994 8
    2980.80.80.984 8
    Table 1. Quenching constants of ACE with LKP at different temperatures
    T/
    K
    nKa/
    (L·mol-1)
    ΔH/
    (KJ·mol-1)
    ΔCp/
    (KJ·mol-1·K-1)
    ΔG/
    (KJ·mol-1)
    -TΔS/
    (KJ·mol-1)
    2880.1312.2×1031 890-18.425 9-1 908.43
    2931.3230.9×1031 118-99.4-16.571-1 134.57
    2981.7275.3×103895.8-21.260 3-917.06
    Table 2. Thermodynamics parameter of binding of LKP and ACE
    Xiao-qing XU, Qian ZHOU, Jian-hua SUN, Li-xia SUN, Xue-zhen FENG, Yong-fang XU, Zhang-fa TONG, Dan-kui LIAO. Study on the Inhibition Mechanism of Angiotensin Conversion Enzyme Inhibitor Peptide Leu-Lys-Pro[J]. Spectroscopy and Spectral Analysis, 2022, 42(7): 2107
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