TY - GEN
T1 - Inhibition potency of HMGR enzyme against hypercholesterolemia by bioactive peptides of CSN1S2 protein from caprine milk
AU - Fatchiyah, Fatchiyah
AU - Natasia, Shella Clarista
N1 - Publisher Copyright:
© 2018 Author(s).
PY - 2018/10/17
Y1 - 2018/10/17
N2 - The most common medications use statin as a remedy for hypercholesterolemia. Statin reduces cholesterol levels by inhibiting the 3-hydroxy-3-methylglutaryl (HMG) CoA reductase (HMGR) enzyme. Unfortunately, statin medication has side effects. This study explores natural hypercholesterolemia remedies without any side effects such as the bioactive peptide of the CSN1S2 protein from Etawah goat milk. In particular, this study analyzes the potential bioactive peptide of CSN1S2 protein as an HMGR inhibitor in silico. The 3D structure of HMGR obtained from the PDB database (ID: 1DQ9) was docked to eight bioactive peptides of CSN1S2 protein from Etawah goat milk using ClusPro. The docking results were visualized and analyzed by Discovery Studio, PyMol, and LigPlot+. The docking results show that three out of eight bioactive peptides of CSN1S2 protein fragments can interact with HMGR. These fragments were 41-NMAIHPR-47, 214-TNAIPVYR-221, and 214- TNAIPYVRL-223. These three fragments interact at residue E559, D767, H866, and especially at cis-loop, residues number 684 through 692. Fragment 41-NMAIHPR-47 has 17 hydrogen bonds with binding energy - 634.8 kJ/mol, fragment 214-TNAIPVYR-221 had 21 hydrogen bonds with binding energy - 765.6 kJ/mol, and fragment 214-TNAIPYVRL-223 had 24 hydrogen bonds with binding energy - 1010.4 kJ/mol. The study results indicate that these three bioactive peptides have the potential to be HMGR inhibitors with low binding energy.
AB - The most common medications use statin as a remedy for hypercholesterolemia. Statin reduces cholesterol levels by inhibiting the 3-hydroxy-3-methylglutaryl (HMG) CoA reductase (HMGR) enzyme. Unfortunately, statin medication has side effects. This study explores natural hypercholesterolemia remedies without any side effects such as the bioactive peptide of the CSN1S2 protein from Etawah goat milk. In particular, this study analyzes the potential bioactive peptide of CSN1S2 protein as an HMGR inhibitor in silico. The 3D structure of HMGR obtained from the PDB database (ID: 1DQ9) was docked to eight bioactive peptides of CSN1S2 protein from Etawah goat milk using ClusPro. The docking results were visualized and analyzed by Discovery Studio, PyMol, and LigPlot+. The docking results show that three out of eight bioactive peptides of CSN1S2 protein fragments can interact with HMGR. These fragments were 41-NMAIHPR-47, 214-TNAIPVYR-221, and 214- TNAIPYVRL-223. These three fragments interact at residue E559, D767, H866, and especially at cis-loop, residues number 684 through 692. Fragment 41-NMAIHPR-47 has 17 hydrogen bonds with binding energy - 634.8 kJ/mol, fragment 214-TNAIPVYR-221 had 21 hydrogen bonds with binding energy - 765.6 kJ/mol, and fragment 214-TNAIPYVRL-223 had 24 hydrogen bonds with binding energy - 1010.4 kJ/mol. The study results indicate that these three bioactive peptides have the potential to be HMGR inhibitors with low binding energy.
UR - https://www.scopus.com/pages/publications/85056167943
U2 - 10.1063/1.5062812
DO - 10.1063/1.5062812
M3 - Conference contribution
AN - SCOPUS:85056167943
T3 - AIP Conference Proceedings
BT - 8th Annual Basic Science International Conference
A2 - Karim, Corina
A2 - Azrianingsih, Rodliyati
A2 - Pamungkas, Mauludi Ariesto
A2 - Jatmiko, Yoga Dwi
A2 - Safitri, Anna
PB - American Institute of Physics Inc.
T2 - 8th Annual Basic Science International Conference: Coverage of Basic Sciences toward the World's Sustainability Challanges, BaSIC 2018
Y2 - 6 March 2018 through 7 March 2018
ER -