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Flexible Molecular Docking of Interaction between Angiotensin Ⅰ-Converting Enzyme (ACE) Inhibitory Dipeptides and ACE

GUAN Xiao1, LIU Jing2,*, SU Xina1, HAN Fei3, WANG Wengao4,5, SHEN Ruiling6, LI Jingjun7, LIAO Lili8   

  1. 1. School of Medical Instrument and Food Engineering, University of Shanghai for Science and Technology, Shanghai 200093,
    China; 2. College of Information Engineering, Shanghai Maritime University, Shanghai 200135, China;
    3. Academy of State Administration of Grain, Beijing 100037, China; 4. Shanghai Liangyou (Group) Co. Ltd., Shanghai 200333,
    China; 5. Shanghai Grain Science Research Institute, Shanghai 200333, China; 6. School of Food and Bioengineering,
    Zhengzhou University of Light Industry, Zhengzhou 450002, China; 7. Jiangsu Changshou (Group) Co. Ltd., Rugao 226500, China;
    8. Guilin Ximai Food Company, Guilin 541004, China
  • Online:2015-03-15 Published:2015-03-17

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Abstract:

AngiotensinⅠ-converting enzyme (ACE) inhibitory peptides are ideal anti-hypertension drugs because they
can inhibit ACE activity in vivo effectively, and have strong blood-reducing activity without side effects. However,
their molecular mechanism remains unclear so far. In this paper, four typical ACE inhibitory dipeptides including GF
(Gly-Phe), GY (Gly-Tyr), VF (Val-Phe) and IY (Ile-Tyr) were chosen as research targets, and their action modes and
molecular mechanisms on ACE were studied in detail by flexible molecular docking method. The results showed that
hydrogen bond, hydrophobic, hydrophilic and electrostatic interactions existed between peptides and ACE, in which hydrogen
bond interaction plays the dominant role. Moreover, Ala354, Glu384 and Arg522 in ACE were especially important binding site
with active peptides, and N-terminal amino groups were the key groups in dipeptides. This information will be helpful for the
molecule design of new ACE inhibitory peptides with strong activity.

Key words: angiotensin Ⅰ-converting enzyme, inhibitory dipeptides, molecular docking, molecular mechanism

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