The inhibitory activity of HL-7 and HL-10 peptide from scorpion venom (Hemiscorpius lepturus) on angiotensin converting enzyme: Kinetic and docking study |
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| Institution: | 1. Department of Organic Chemistry, Kaunas University of Technology, LT-50254, Radvil?n? pl. 19, Kaunas, Lithuania;2. Department of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saul?tekio 7, Vilnius LT-10257, Lithuania;3. Department of Physical and Inorganic Chemistry, Kaunas University of Technology, LT-50254, Radvil?n? pl. 19, Kaunas, Lithuania;1. Department of Chemistry, Quaid-i-Azam University, Islamabad 45320, Pakistan;2. Centre for Advanced Drug Research, COMSATS Institute of Information Technology, Abbottabad 22060, Pakistan;3. Cardiovascular and Metabolic Research Unit, Laurentian University, Sudbury, ON P3E2C6, Canada;1. H.E.J. Research Institute of Chemistry, International Center for Chemical and Biological Sciences, University of Karachi, Karachi 75270, Pakistan;2. Center for Advanced Drug Research, COMSATS Institute of Information Technology, Abbottabad 22060, Pakistan;3. Dr. Panjwani Center for Molecular Medicine and Drug Research, International Center for Chemical and Biological Sciences, University of Karachi, Karachi 75270, Pakistan;4. Institute of Chemistry, The University of the Punjab, Lahore 54000, Pakistan;1. International Chinese-Belorussian Scientific Laboratory on Vacuum-Plasma Technology, College of Chemical Engineering, Nanjing University of Science and Technology, Nanjing 210094, China;2. Francisk Skorina Gomel State University, 104, Sovetskaya Street, Gomel 246019, Belarus;1. Transplantation Laboratory, Medicum, University of Helsinki, Finland;2. Raasepori Health Care Centre, Raasepori, Finland;3. University of Helsinki, Helsinki, Finland |
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| Abstract: | The hypertension is one of the highest risk factors for stroke, myocardial infarction, vascular disease and chronic kidney disease. Angiotensin converting enzyme (ACE) has an important role in the physiological regulation of cardiovascular system. ACE inhibition is a key purpose for hypertension treatment. In this study, two peptides named HL-7 with the sequence of YLYELAR (MW: 927.07 Da) and HL-10 with the sequence of AFPYYGHHLG (MW: 1161.28 Da) were identified from scorpion venom of H. lepturus. The inhibitory activity of HL-7 and HL-10 was examined on rabbit ACE. The inhibition mechanisms were assayed by kinetic and docking studies. The IC50 values for ACE inhibition of HL-7 and HL-10 were 9.37 µM and 17.22 µM, respectively. Lineweaver-Burk plots showed that two peptides inhibited rabbit ACE with competitive manner. The molecular docking conformed experimental results and showed that the two peptides interacted with N-domain and C-domain active sites. Also, docking study revealed that the two peptides can form hydrogen and hydrophobic bonds at their binding sites. Both peptides had higher affinity to N-domain. Our results showed that HL-7 exhibited more strong interactions with amino acids at active site. It seems that HL-10 peptide could occupy more space, thereby inhibiting the substrate entrance to active site. |
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| Keywords: | Scorpion venom peptide ACE Molecular docking Inhibition Blood pressure |
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